Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. 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, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including 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. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      20 QVTQSSPEQRVASGREVTLQCTFQTTYSNPDLYWYRKTPDAVFQFVLYRDntrSRDADFARGRFTVQHSVRSKTFHLVIS 99
Cdd:cd07706   1 KVTQAQPDVSVQVGEEVTLNCRYETSWTNYYLFWYKQLPSGEMTFLIRQD---SSEQNAKSGRYSVNFQKAQKSISLTIS 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2259     100 SVRPEDTATYYCALdlqRGIYDtTDKLTFGKGTRLIVEP 138
Cdd:cd07706  78 ALQLEDSAKYFCAL---SLPYD-TDKLIFGKGTRLTVEP 112

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      20 QVTQSSPEQRVASGREVTLQCTFQTTYSNPDLYWYRKTPDAVFQFVLYRDntrSRDADFARGRFTVQHSVRSKTFHLVIS 99
Cdd:cd07706   1 KVTQAQPDVSVQVGEEVTLNCRYETSWTNYYLFWYKQLPSGEMTFLIRQD---SSEQNAKSGRYSVNFQKAQKSISLTIS 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2259     100 SVRPEDTATYYCALdlqRGIYDtTDKLTFGKGTRLIVEP 138
Cdd:cd07706  78 ALQLEDSAKYFCAL---SLPYD-TDKLIFGKGTRLTVEP 112

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2259         36 VTLQCTF-QTTYSNPDLYWYRKTPDAVFQFVLYRDNTRSR-DADFARGRFTVQHSVRSKTFHLVISSVRPEDTATYYCA 112
Cdd:smart00406   2 VTLSCKFsGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSyYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCA 80

Immunoglobulin (Ig) variable (V) domain of T-cell receptor (TCR) delta chain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the delta chain of gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      20 QVTQSSPEQRVASGREVTLQCTFQTTYSNPDLYWYRKTPDAVFQFVLYRDntrSRDADFARGRFTVQHSVRSKTFHLVIS 99
Cdd:cd07706   1 KVTQAQPDVSVQVGEEVTLNCRYETSWTNYYLFWYKQLPSGEMTFLIRQD---SSEQNAKSGRYSVNFQKAQKSISLTIS 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2259     100 SVRPEDTATYYCALdlqRGIYDtTDKLTFGKGTRLIVEP 138
Cdd:cd07706  78 ALQLEDSAKYFCAL---SLPYD-TDKLIFGKGTRLTVEP 112

Immunoglobulin variable domain (IgV); The members here are composed of the immunoglobulin variable domain (IgV). The IgV family contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology, and 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. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E and, D strands in one sheet and A', G, F, C, C', and C" strands in the other.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      21 VTQSSPEQRVASGREVTLQCTFQTTYSNPDLYWYRKTPDAVFQFVLYRDNTRSRDADFARGRFTVQHSvRSKTFHLVISS 100
Cdd:cd00099   1 VTQSPRSLSVQEGESVTLSCEVSSSFSSTYIYWYRQKPGQGPEFLIYLSSSKGKTKGGVPGRFSGSRD-GTSSFSLTISN 79

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 2259     101 VRPEDTATYYCALDLQRGiydtTDKLTFGKGTRLIV 136
Cdd:cd00099  80 LQPEDSGTYYCAVSESGG----TDKLTFGSGTRLTV 111

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259        23 QSSPEQRVASGREVTLQCTFQTTYSNPDL--YWYRKTPDAVFQFVLYRdNTRSRDADFARGRFTVQHSVRSKTFHLVISS 100
Cdd:pfam07686   1 QTPREVTVALGGSVTLPCTYSSSMSEASTsvYWYRQPPGKGPTFLIAY-YSNGSEEGVKKGRFSGRGDPSNGDGSLTIQN 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2259       101 VRPEDTATYYCALdlqrgiyDTTDKLTFGKGTRLIV 136
Cdd:pfam07686  80 LTLSDSGTYTCAV-------IPSGEGVFGKGTRLTV 108

Immunoglobulin V-Type;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2259         36 VTLQCTF-QTTYSNPDLYWYRKTPDAVFQFVLYRDNTRSR-DADFARGRFTVQHSVRSKTFHLVISSVRPEDTATYYCA 112
Cdd:smart00406   2 VTLSCKFsGSTFSSYYVSWVRQPPGKGLEWLGYIGSNGSSyYQESYKGRFTISKDTSKNDVSLTISNLRVEDTGTYYCA 80

Immunoglobulin (Ig) lambda light chain variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, lambda type, variable (V) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      21 VTQSSPEQrVASGREVTLQCTFQT-TYSNPDLYWYRKTPDAVFQFVLYRDNTRSrdaDFARGRFTvqHSVRSKTFHLVIS 99
Cdd:cd04984   2 LTQPSSLS-VSPGETVTITCTGSSgNISGNYVNWYQQKPGSAPRYLIYEDKHRP---SGIPDRFS--GSKSGNTASLTIS 75

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 2259     100 SVRPEDTATYYCAldlqrgIYDTTDkLTFGKGTRLIV 136
Cdd:cd04984  76 GAQTEDEADYYCQ------VWDSNS-YVFGGGTKLTV 105

Immunoglobulin (Ig) light chain, kappa type, variable (V) domain; The members here are composed of the immunoglobulin (Ig) light chain, kappa type, variable (V) domain. This group contains the standard Ig superfamily V-set AGFCC'C"/DEB domain topology. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. There are two types of light chains: kappa and lambda, each composed of a constant domain (CL) and a variable domain (VL). There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determines the type of immunoglobulin formed: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      20 QVTQSSPEQRVASGREVTLQCTFQTTYSNPDLYWYRKTPDAVFQFVLYRDNTRsrdADFARGRFTVQHSvrSKTFHLVIS 99
Cdd:cd04980   2 VMTQSPASLSVSPGERVTISCKASQSISSNYLAWYQQKPGQAPKLLIYYASTL---HSGVPSRFSGSGS--GTDFTLTIS 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 2259     100 SVRPEDTATYYCaldLQrgiYDTTdKLTFGKGTRL 134
Cdd:cd04980  77 SVEPEDAAVYYC---QQ---GYTF-PYTFGGGTKL 104

Gammadelta T-cell antigen receptor, variable (V) domain; The members here are composed of the immunoglobulin (Ig) variable (V) domain of the gamma/delta T-cell receptors (TCRs). TCRs mediate antigen recognition by T lymphocytes, and are heterodimers consisting of alpha and beta chains or gamma and delta chains. Each chain contains a variable (V) and a constant (C) region. The majority of T cells contain alpha/beta TCRs, but a small subset contain gamma/delta TCRs. Alpha/beta TCRs recognize antigen as peptide fragments presented by major histocompatibility complex (MHC) molecules. Gamma/delta TCRs recognize intact protein antigens; they recognize protein antigens directly and without antigen processing, and MHC independently of the bound peptide. Gamma/delta T cells can also be stimulated by non-peptide antigens such as small phosphate- or amine-containing compounds. The variable domain of gamma/delta TCRs is responsible for antigen recognition and is located at the N-terminus of the receptor. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      30 VASGREVTLQCTFQ-TTYSNPDLYWYRKTPDAVFQFVlYRDNTRSRDADFARGRFTVQHSVRSKTFHLVISSVRpeDTAT 108
Cdd:cd20988  10 VSVGKPVTLKCSMKgEAISNYYINWYRKTQGNTMTFI-YREGGIYGPGFKDNFRGDIDSSNNLAVLKILEASER--DEGS 86

                        90       100
                ....*....|....*....|....*....
gi 2259     109 YYCALDlQRGIYDTTDKLTFGKGTRLIVE 137
Cdd:cd20988  87 YYCASD-TPGGGREYDPLIFGKGTYLTVE 114

Immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1); The members here are composed of the immunoglobulin (Ig)-like domain of Programmed Cell Death 1 (PD1; also known as CD279/cluster of differentiation 279). PD1 is a cell surface receptor that is expressed on T cells and pro-B cells. The protein's structure includes an extracellular IgV domain followed by a transmembrane region and an intracellular tail. Activation of CD4+ T cells, CD8+ T cells, NKT cells, B cells, and monocytes induces PD-1 expression, immediately after which it binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274/cluster of differentiation 274) and PD-L2, also known as B7-DC. PD-1 plays an important role in down regulating the immune system by preventing the activation of T-cells, reducing autoimmunity and promoting self-tolerance. The inhibitory effect of PD-1 is accomplished by promoting apoptosis in antigen specific T-cells in lymph nodes while simultaneously reducing apoptosis in regulatory T cells. A class of drugs that target PD-1, known as the PD-1 inhibitors, activate the immune system to attack tumors and treat cancer. Comparisons between the mouse PD-1 (mPD-1) and human PD-1 (hPD-1) reveals that unlike the mPD-1 which has a conventional IgSF V-set domain, hPD-1 lacks a C" strand, and instead the C' and D strands are connected by a long and flexible loop. In addition, the BC loop is not stabilized by disulfide bonding to the F strand of the ligand binding beta sheet. These differences result in different binding affinities of human and mouse PD-1 for their ligands.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      24 SSPEQ-RVASGREVTLQCTFQTTYSNPDLYWYRKTPdavfqfvlyrDNTRSRDADFA--------RGRFTVQHSVRSKTF 94
Cdd:cd16088   4 FSPALlVVTEGANATFTCSFSNTSESFVLNWYRLSP----------SNQTDKLAAFPedrsqpgqDWRFRVTQLPNGRDF 73

                        90
                ....*....|....*...
gi 2259      95 HLVISSVRPEDTATYYCA 112
Cdd:cd16088  74 HMSVVRARRNDSGTYLCG 91

Immunoglobulin variable (IgV) domain of Natural Killer cell activating receptor NKp30 and similar domains; The members here are composed of the immunoglobulin variable region (IgV) of Natural Killer cell activating receptor NKp30 (also known as Natural Cytotoxicity triggering Receptor 3 (NCR3)) and similar domains. NKp30 Recognizes the N-Terminal IgV Domain of B7-H6. In humans, the activating natural cytotoxicity receptor NKp30 plays a major role in NK cell-mediated tumor cell lysis. NKp30 recognizes the cell-surface protein B7-H6, which is expressed on tumor, but not healthy, cells.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      26 PEQRVASGREVTLQCTFQTTYSNP---DLYWYRktpDAVFQFVLYRDNT---RSRDADFARGRFTVQHSVrsktfHLVIS 99
Cdd:cd20926   8 PEIRTLEGSSAFLPCSFNASQGRLaigSVTWFR---DEVAPGKEVRNGTpefRGRLAPLASSRFLRDHQA-----ELHIW 79

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 2259     100 SVRPEDTATYYCALD-LQRGIydttdklTFGKGTRLIVE 137
Cdd:cd20926  80 DVRGHDAGIYVCRVEvLGLGV-------GTGNGTRLVVE 111

Immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain in the polymeric Ig receptor (pIgR) and similar proteins. pIgR delivers dimeric IgA and pentameric IgM to mucosal secretions. Polymeric immunoglobulin (pIgs) are the first defense against pathogens and toxins. IgA and IgM can form polymers via an 18-residue extension at their C-termini referred to as the tailpiece. pIgR transports pIgs across mucosal epithelia into mucosal secretions. Human pIgR is a glycosylated type I transmembrane protein, comprised of a 620-residue extracellular region, a 23-residue transmembrane region, and a 103-residue cytoplasmic tail. The extracellular region contains five domains that share sequence similarity with Ig variable (v) regions. This group also contains the Ig-like extracellular domains of other receptors such as NK cell receptor Nkp44 and myeloid receptors, among others.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      33 GREVTLQCTFQTTYSNPDLYWYR---KTPDAVFqfvlyrdntrSRDADFARGRFTVQHSVRSKTFHLVISSVRPEDTATY 109
Cdd:cd05716  12 GGSVTIQCPYPPKYASSRKYWCKwgsEGCQTLV----------SSEGVVPGGRISLTDDPDNGVFTVTLNQLRKEDAGWY 81

                        90
                ....*....|....*...
gi 2259     110 YCALDlQRGIYDTTDKLT 127
Cdd:cd05716  82 WCGVG-DDGDRGLTVQVK 98

Immunoglobulin Variable (IgV) domain at the N-terminus of CD33 and related Siglecs (sialic acid-binding Ig-like lectins); The members here are composed of the immunoglobulin (Ig) domain at the N-terminus of Cluster of Differentiation (CD) 33 and related Siglecs (sialic acid-binding Ig-like lectins). Siglec refers to a structurally related protein family that specifically recognizes sialic acid in oligosaccharide chains of glycoproteins and glycolipids. Siglecs are type I transmembrane proteins, organized as an extracellular module composed of Ig-like domains, an N-terminal variable set of Ig-like carbohydrate recognition domains, and 1 to 16 constant Ig-like domains, followed by transmembrane and short cytoplasmic domains. Human Siglecs are classified into two subgroups, one subgroup is comprised of sialoadhesin (Siglec-1), CD22 (Siglec-2), and MAG, the other subgroup is comprised of CD33-related Siglecs which include CD33 (Siglec-3) and human Siglecs 5-11.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      30 VASGREVTLQCTFQ---TTYSNPDL--YWYRKTPD-AVFQFVLYRDNTRSRDADFaRGRFTVQHSVRSKTFHLVISSVRP 103
Cdd:cd05712  11 VQEGLCVLIPCSFSypaDYWVSNPVhgYWYRGGPYpKYRPPVATNNRTREVHEST-QGRFRLLGDPGKKNCSLSISDARP 89

                        90
                ....*....|..
gi 2259     104 EDTATYYCALDL 115
Cdd:cd05712  90 EDSGKYFFRVER 101

Immunoglobulin (Ig)-like variable (V) domain of Cluster of Differentiation (CD) 8 alpha chain; The members here are composed of the immunoglobulin (Ig)-like variable domain of the Cluster of Differentiation (CD) 8 alpha. The CD8 glycoprotein plays an essential role in the control of T-cell selection, maturation, and the T-cell receptor (TCR)-mediated response to peptide antigen. CD8 is comprised of alpha and beta subunits and is expressed as either an alpha/alpha or alpha/beta dimer. Both dimeric isoforms can serve as a coreceptor for T cell activation and differentiation, however they have distinct physiological roles, different cellular distributions, unique binding partners, etc. Each CD8 subunit is comprised of an extracellular domain containing a V-type Ig-like domain, a single pass transmembrane portion, and a short intracellular domain. The Ig domain of CD8 alpha binds to antibodies. Members of this group contain standard Ig superfamily V-set AGFCC'C"/DEB domain topology.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2259      25 SPEQRVAS-GREVTLQCtfQTTYSNPD-LYWYRKTPDAVFQ--FVLYRdnTRSRDADFARG----RFTVQHSvrSKTFHL 96
Cdd:cd05720   4 SPRKRDAQlGQKVELVC--EVLNSVPQgCSWLFQPRGSAPQptFLLYL--SSSNKTKWAEGldskRFSGSRS--GSSYVL 77

                        90
                ....*....|....*
gi 2259      97 VISSVRPEDTATYYC 111
Cdd:cd05720  78 TLKDFRKEDEGYYFC 92

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. 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, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including 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. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2259      36 VTLQCTFqTTYSNPDLYWYRktpdavfqfvlyrdNTRSRDADFARGRFTVQHSvrsktFHLVISSVRPEDTATYYC 111
Cdd:cd00096   1 VTLTCSA-SGNPPPTITWYK--------------NGKPLPPSSRDSRRSELGN-----GTLTISNVTLEDSGTYTC 56