NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|161484599|ref|NP_062261|]
View 

T-lymphocyte activation antigen CD86 precursor [Mus musculus]

Protein Classification

IgV_CD86 domain-containing protein( domain architecture ID 11610713)

IgV_CD86 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
26-133 1.17e-70

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


:

Pssm-ID: 409508  Cd Length: 108  Bit Score: 214.11  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  26 VETQAYFNGTAYLPCPFTKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSVNAKYLGRTSFDRNNWTLRLHNVQIKDM 105
Cdd:cd16087    1 LKIQAYFNETAYLPCQFKNPQNISLSELVVFWQDQKKLVLYELYLGKEKLDNVNSKYIGRTSFDQENWTLQLHNVQIKDQ 80
                         90       100
                 ....*....|....*....|....*...
gi 161484599 106 GSYDCFIQKKPPTGSIILQQTLTELSVI 133
Cdd:cd16087   81 GTYQCFIHHKSPKGLVLIHQMSSELSVI 108
 
Name Accession Description Interval E-value
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
26-133 1.17e-70

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 214.11  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  26 VETQAYFNGTAYLPCPFTKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSVNAKYLGRTSFDRNNWTLRLHNVQIKDM 105
Cdd:cd16087    1 LKIQAYFNETAYLPCQFKNPQNISLSELVVFWQDQKKLVLYELYLGKEKLDNVNSKYIGRTSFDQENWTLQLHNVQIKDQ 80
                         90       100
                 ....*....|....*....|....*...
gi 161484599 106 GSYDCFIQKKPPTGSIILQQTLTELSVI 133
Cdd:cd16087   81 GTYQCFIHHKSPKGLVLIHQMSSELSVI 108
IGv smart00406
Immunoglobulin V-Type;
35-112 5.69e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.08  E-value: 5.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599    35 TAYLPCpftKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSV--NAKYLGRTSF----DRNNWTLRLHNVQIKDMGSY 108
Cdd:smart00406   1 SVTLSC---KFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSyyQESYKGRFTIskdtSKNDVSLTISNLRVEDTGTY 77

                   ....
gi 161484599   109 DCFI 112
Cdd:smart00406  78 YCAV 81
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
24-132 1.74e-04

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 40.13  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599   24 VSVETQAYFNGTAYLPCPFTKaqNISLSELVVFW------QDQQKLVLYEHYLGTEKLDSvnAKYLGRTSFDRNNWTLRL 97
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSS--SMSEASTSVYWyrqppgKGPTFLIAYYSNGSEEGVKK--GRFSGRGDPSNGDGSLTI 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 161484599   98 HNVQIKDMGSYDCFIQKKPPTGSiilqQTLTELSV 132
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSGEGVF----GKGTRLTV 108
 
Name Accession Description Interval E-value
IgV_CD86 cd16087
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here ...
26-133 1.17e-70

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 86; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 86). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. The CTLA-4 and B7-2 monomers are both two-layer beta-sandwiches that display the chain topology characteristic of the immunoglobulin variable (V-type) domains present in antigen receptors. The front and back sheets of B7-2 are composed of AGFCC'C" and BED strands, respectively. Members of the IgV family are components of immunoglobulin (Ig) and T cell receptors. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. Within the variable domain, there are regions of even more variability called the hypervariable or complementarity-determining regions (CDRs) which are responsible for antigen binding. A predominant feature of most Ig domains is the disulfide bridge connecting 2 beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409508  Cd Length: 108  Bit Score: 214.11  E-value: 1.17e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  26 VETQAYFNGTAYLPCPFTKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSVNAKYLGRTSFDRNNWTLRLHNVQIKDM 105
Cdd:cd16087    1 LKIQAYFNETAYLPCQFKNPQNISLSELVVFWQDQKKLVLYELYLGKEKLDNVNSKYIGRTSFDQENWTLQLHNVQIKDQ 80
                         90       100
                 ....*....|....*....|....*...
gi 161484599 106 GSYDCFIQKKPPTGSIILQQTLTELSVI 133
Cdd:cd16087   81 GTYQCFIHHKSPKGLVLIHQMSSELSVI 108
IGv smart00406
Immunoglobulin V-Type;
35-112 5.69e-10

Immunoglobulin V-Type;


Pssm-ID: 214650  Cd Length: 81  Bit Score: 55.08  E-value: 5.69e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599    35 TAYLPCpftKAQNISLSELVVFWQDQQKLVLYEHYLGTEKLDSV--NAKYLGRTSF----DRNNWTLRLHNVQIKDMGSY 108
Cdd:smart00406   1 SVTLSC---KFSGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSyyQESYKGRFTIskdtSKNDVSLTISNLRVEDTGTY 77

                   ....
gi 161484599   109 DCFI 112
Cdd:smart00406  78 YCAV 81
IgV_B7-H4 cd20984
Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the ...
30-119 7.46e-10

Immunoglobulin Variable (IgV) domain of B7-H4; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H4 (also known as B7-S1, B7x, or Vtcn1). B7-H4 is one of the B7 family of immune-regulatory ligands that act as negative regulators of T cell function; it contains one IgV domain and one IgC domain. The B7-family consists of structurally related cell-surface protein ligands, which bind to receptors on lymphocytes that regulate immune responses. The binding of B7-H4 to unidentified receptors results in the inhibition of TCR-mediated T cell proliferation, cell-cycle progression and IL-2 production. As a co-inhibitory molecule, B7-H4 is widely expressed in tumor tissues and its expression is significantly associated with poor prognosis in human cancers such as glioma, pancreatic cancer, oral squamous cell carcinoma, renal cell carcinoma, and lung cancer.


Pssm-ID: 409576  Cd Length: 110  Bit Score: 55.68  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  30 AYFNGTAYLPCPFTKaqNISLSELVVFWQDQQKL-VLYEHYLGTEKLDSVNAKYLGRTSF-----DRNNWTLRLHNVQIK 103
Cdd:cd20984    9 GNIGEDGILSCTFTP--DIKLSDIVIQWLKEGDSgLVHEFKEGKDELSRQSPMFRGRTSLfadqvHVGNASLRLKNVQLT 86
                         90
                 ....*....|....*.
gi 161484599 104 DMGSYDCFIQKKPPTG 119
Cdd:cd20984   87 DAGTYLCIISNSKGTG 102
IgV_B7-H3 cd20934
Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint ...
30-124 2.74e-09

Immunoglobulin Variable (IgV) domain of B7-H3, a member of the B7 family of immune checkpoint molecules; The members here are composed of the immunoglobulin variable (IgV) domain of B7-H3 also known as CD276), a member of the B7 family of immune checkpoint molecules. B7-H3 is an important immune checkpoint member of the B7 family and shares homology with other B7 ligands such as programmed death ligand 1 (PD-L1). The B7 family molecules interact with CD28 on T-cells to provide co-stimulatory signals that regulate T-cell activation and T-helper cell differentiation. Although B7-H3 has been shown to have both co-stimulatory and co-inhibitory effects on T-cell responses, the most current studies describe B7-H3 as a T cell inhibitor that promotes tumor aggressiveness and proliferation. Moreover, B7-H3 is highly overexpressed on a wide range of human solid cancers and promotes tumor growth, metastasis, and drug resistance. Thus, B7-H3 expression in tumors often correlates with both negative prognosis and poor clinical outcome in cancer patients. B7-H3 protein contains a predicted signal peptide, V- and C-like Ig domains (IgV and IgC), a transmembrane region, and an intracellular tail.


Pssm-ID: 409528  Cd Length: 115  Bit Score: 54.15  E-value: 2.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  30 AYFNGTAYLPCPFTKAQNISLSELVVFWQ--DQQKLVlYEHYLGTEKLDSVNAKYLGRTS-----FDRNNWTLRLHNVQI 102
Cdd:cd20934    9 ALVGTDATLRCSFSPEPGFSLAQLSVFWQltDTKQLV-HSFTESQDQGRDQGSAYANRTAlfpdlLAQGNASLRLQRVRV 87
                         90       100
                 ....*....|....*....|...
gi 161484599 103 KDMGSYDCFIQ-KKPPTGSIILQ 124
Cdd:cd20934   88 ADEGSYTCFVSvQDFGSAAVSLQ 110
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
38-112 1.04e-08

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 52.39  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  38 LPCPFTKAqnislSELVVFWQDQQ-KLVLYEHYLGTEKLDSVNAKYLGRTSFDRN-----NWTLRLHNVQIKDMGSYDCF 111
Cdd:cd16091   17 LPCSFTPG-----SEVVIHWYKQDsDIKVHSYYYGKDQLESQDQRYRNRTSLFKDqisngNASLLLRRVQLQDEGRYKCY 91

                 .
gi 161484599 112 I 112
Cdd:cd16091   92 T 92
IgV_MOG_like cd05713
Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here ...
34-133 1.11e-06

Immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG); The members here are composed of the immunoglobulin (Ig)-like domain of myelin oligodendrocyte glycoprotein (MOG). MOG, a minor component of the myelin sheath, is an important CNS-specific autoantigen, linked to the pathogenesis of multiple sclerosis (MS) and experimental autoimmune encephalomyelitis (EAE). It is a transmembrane protein having an extracellular Ig domain. MOG is expressed in the CNS on the outermost lamellae of the myelin sheath, and on the surface of oligodendrocytes, and may participate in the completion, compaction, and/or maintenance of myelin. This group also includes butyrophilin (BTN). BTN is the most abundant protein in bovine milk-fat globule membrane (MFGM).


Pssm-ID: 409378  Cd Length: 114  Bit Score: 46.80  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  34 GTAYLPCPFTKAQNISLSElVVFWQDQQKLV--LYEHylGTEKLDSVNAKYLGRTSFDRN-----NWTLRLHNVQIKDMG 106
Cdd:cd05713   16 EDAELPCHLSPKMSAEHME-VRWFRSQFSPVvhLYRD--GQDQEEEQMPEYRGRTELLKDaiaegSVALRIHNVRPSDEG 92
                         90       100
                 ....*....|....*....|....*..
gi 161484599 107 SYDCFIQKkpptgSIILQQTLTELSVI 133
Cdd:cd05713   93 QYTCFFRS-----GSFYEEATLELKVA 114
IgV_CD80 cd16086
Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here ...
36-115 4.43e-06

Immunoglobulin variable domain (IgV) in Cluster of Differentiation (CD) 80; The members here are composed of the immunoglobulin variable region (IgV) in the Cluster of Differentiation (CD) 80). Glycoproteins B7-1 (also known as cluster of differentiation (CD) 80) and B7-2 (also known as CD86) are expressed on antigen-presenting cells and deliver the co-stimulatory signal through CD28 and CTLA-4 (also known as cluster of differentiation 152/CD152) on T cells. signaling through CD28 augments the T-cell response, whereas CTLA-4 signaling attenuates it. CD80 contains two Ig-like domains, an amino-terminal immunoglobulin variable (IgV)-like domain characteristic of adhesion molecules and a membrane proximal immunoglobulin constant (IgC)-like domain similar to the constant domains of antigen receptors. Members of the Ig family are components of immunoglobulin, T-cell receptors, CD1 cell surface glycoproteins, secretory glycoproteins A/C, and Major Histocompatibility Complex (MHC) class I/II molecules. In immunoglobulins, each chain is composed of one variable domain (IgV) and one or more IgC domains. These names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. The IgV domain is responsible for antigen binding, and the IgC domain is involved in oligomerization and molecular interactions.


Pssm-ID: 319335  Cd Length: 105  Bit Score: 44.75  E-value: 4.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  36 AYLPCPFtkaqNISLSELV---VFWQDQQKLVLYehyLGTEKLdSVNAKYLGRTSFD-RNNWTLRLHNVQIKDMGSYDCF 111
Cdd:cd16086   12 ALLSCDY----NVSVDELAqvrIYWQKDDKMVLT---IISGDV-KVWPEYKNRTLFDiTNNLSIVILALRLSDRGTYTCV 83

                 ....
gi 161484599 112 IQKK 115
Cdd:cd16086   84 VQKK 87
IgV_1_PVR_like cd05718
First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 ...
24-132 5.04e-05

First immunoglobulin variable (IgV) domain of poliovirus receptor (PVR, also known as CD155 and necl-5), and similar domains; The members here are composed of the first immunoglobulin (Ig) domain of poliovirus receptor (PVR, also known as CD155 and nectin-like protein 5 (necl-5)). Poliovirus (PV) binds to its cellular receptor (PVR/CD155) to initiate infection. CD155 is a membrane-anchored, single-span glycoprotein; its extracellular region has three Ig-like domains. There are four different isotypes of CD155 (referred to as alpha, beta, gamma, and delta), that result from alternate splicing of the CD155 mRNA, and have identical extracellular domains. CD155-beta and CD155-gamma are secreted; CD155-alpha and CD155-delta are membrane-bound and function as PV receptors. The virus recognition site is contained in the amino-terminal domain, D1. Having the virus attachment site on the receptor distal from the plasma membrane may be important for successful initiation of infection of cells by the virus. CD155 binds in the poliovirus "canyon" with a footprint similar to that of the intercellular adhesion molecule-1 receptor on human rhinoviruses. This group also includes the first Ig-like domain of nectin-1 (also known as poliovirus receptor related protein(PVRL)1; CD111), nectin-3 (also known as PVRL 3), nectin-4 (also known as PVRL4; LNIR receptor)and DNAX accessory molecule 1 (DNAM-1; CD226).


Pssm-ID: 409383  Cd Length: 113  Bit Score: 42.05  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  24 VSVETQ--AYFNGTAYLPCPFTKAQNISLSElvVFWQ-----DQQKLVLYEHYLGTekldSVNAKYLGRTSF-----DRN 91
Cdd:cd05718    3 VQVPTEvtGFLGGSVTLPCSLTSPGTTKITQ--VTWMkigagSSQNVAVFHPQYGP----SVPNPYAERVEFlaarlGLR 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 161484599  92 NWTLRLHNVQIKDMGSYDC----FiqkkpPTGSiilQQTLTELSV 132
Cdd:cd05718   77 NATLRIRNLRVEDEGNYICefatF-----PQGN---RQGTTWLRV 113
V-set pfam07686
Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 ...
24-132 1.74e-04

Immunoglobulin V-set domain; This domain is found in antibodies as well as neural protein P0 and CTL4 amongst others.


Pssm-ID: 462230  Cd Length: 109  Bit Score: 40.13  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599   24 VSVETQAYFNGTAYLPCPFTKaqNISLSELVVFW------QDQQKLVLYEHYLGTEKLDSvnAKYLGRTSFDRNNWTLRL 97
Cdd:pfam07686   2 TPREVTVALGGSVTLPCTYSS--SMSEASTSVYWyrqppgKGPTFLIAYYSNGSEEGVKK--GRFSGRGDPSNGDGSLTI 77
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 161484599   98 HNVQIKDMGSYDCFIQKKPPTGSiilqQTLTELSV 132
Cdd:pfam07686  78 QNLTLSDSGTYTCAVIPSGEGVF----GKGTRLTV 108
IgV_PDl1 cd20947
Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here ...
38-112 5.73e-04

Immunoglobulin Variable (IgV) domain of Programmed death ligand 1 (PD-L1); The members here are composed of the immunoglobulin variable (IgV) domain of Programmed death ligand 1 (PD-L1; also known as Cluster of Differentiation 274 (CD274)). PD-L1 is a cell-surface ligand that competes with PD-L2 for binding to the immunosuppressive receptor programmed death-1 (PD-1). PD-1 is a member of the B7 family that plays an important role in negatively regulating immune responses upon interaction with its two ligands, PD-L1 or PD-L2. Like PD-L2, PD-L1 interacts with PD-1 and suppresses T cell proliferation and cytokine production. The PD-1 receptor is expressed on the surface of activated T cells, while PD-L1 is expressed on cancer cells. When PD-1 and PD-L1 bind together, they form a molecular shield protecting tumor cells from being destroyed by the immune system. Thus, inhibiting the binding of PD-L1 to PD-1 with an antibody leads to killing of tumor cells by T cells. PD-1 inhibitors (such as Pembrolizumab, Nivolumab, and Cemiplimab) and PD-L1 inhibitors (such as Atezolizumab, Avelumab, and Durvalumab ) are an emerging class of immunotherapy that stimulate lymphocytes against tumor cells.


Pssm-ID: 409539  Cd Length: 110  Bit Score: 38.76  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 161484599  38 LPCPFTKAQNISLSELVVFWQDQQKLVLyEHYLGTEKLDSVNAKYLGRTSFDRN-----NWTLRLHNVQIKDMGSYDCFI 112
Cdd:cd20947   18 IECKFPVEKQLDLAALIVYWEMEDKNII-QFVHGEEDLKVQHSSYRQRARLLKDqlslgNAALQITDVKLQDAGVYRCMI 96
IgV_CRIg cd16089
Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin ...
80-132 6.50e-03

Immunoglobulin variable (IgV)-like domain in complement receptor of the immunoglobulin superfamily (CRIg); The members here are composed of the immunoglobulin variable (IgV) region of the complement receptor of the immunoglobulin superfamily (CRIg). The N-terminal domain of CRIg (also known as Z39Ig and V-set and Ig domain-containing 4 (VSIG4) belongs to the IgV family of immunoglobulin-like domains while the C-terminal domain of CRIg belongs to the IgC family of immunoglobulin-like domains. Like all members of this family, the CRIg domain contains two beta-sheets: one composed of strands A', G, F, C, C' and C", and the other of strands B, E and D. The complement system is an important part of the innate immune system and is required for removal of pathogens from the bloodstream. After exposure to pathogens, the third component of the complement system, C3, is cleaved to C3b which, after recruitment of factor B, initiates formation of the alternative pathway convertases. CRIg, a complement receptor expressed on macrophages, binds to C3b and iC3b mediating phagocytosis of the particles. It is also a potent inhibitor of the alternative pathway convertases and a negative regulator of T cell activation. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, such as, T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, such as, butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond.


Pssm-ID: 409510  Cd Length: 117  Bit Score: 35.96  E-value: 6.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 161484599  80 AKYLGRTSFDRN---NWTLRLHNVQIKDMGSYDCFIQKKPPTGSIILQQTLTELSV 132
Cdd:cd16089   60 AKYRGRLEVSKDtpgDVSLQLDTLEMDDRGHYTCQVTWQTPDGNLIVREKTTELRV 115
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH