1B08,1HUP,1KX1,1PWB,1R13,1R14,1KZE,1KWY


Conserved Protein Domain Family
CLECT_collectin_like
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cd03591: CLECT_collectin_like 
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C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1)
CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.
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Statistics
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PSSM-Id: 153061
Aligned: 23 rows
Threshold Bit Score: 175.177
Created: 21-Mar-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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Conserved site includes 5 residues -Click on image for an interactive view with Cn3D
Feature 1:carbohydrate binding site [chemical binding site]
Evidence:
  • Structure:1PWB_C, human lung surfactant protein D trimer, bound with maltose and calcium ions , contacts at 3.5A
  • Structure:1KWY_A, rat mannose protein A trimer bound with Man-A13-Man, contacts at 3.5 A.
  • Structure:1KX1_F, rat Mannose Protein A bound with Man6-Glcnac2-Asn and calcium ion, contacts at 3.5 A.
  • Comment:Man6GlcNAcAsn oligosaccharide binds to one protomer of two different trimers of rat MBP-A.
  • Structure:1KZE_2, rat mannose-binding protein C dimer bound with bivalent man-terminated glycopeptide, contacts at 3.5 A
  • Structure:1HUP, human mannose binding protein monomer, bound with a calcium ion and a tetrahedral sulphate ion mimicking the binding of mannose, contacts at 3.5 A
  • Citation:PMID 7634089
  • Structure:1R13_A, rat surfactant protein A (Sp-A) bound with calcium at the primary calcium site, contacts at 3.5 A.
  • Comment:The primary calcium site of rat surfactant protein A (Sp-A) primary is similar to the one found in MBP and SP-D in which two coordination positions are occupied by carbohydrate oxygens. Mannose does not bind here presumably due to competition with the cryoprotectant glycerol.
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                                                                                     
1B08_A     45 EKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVva---knEAAFLSMTDSKTEGKFTYPTGESL--VYSN 119 human
1PWB_C     64 EKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVva---knEAAFLSMTDSKTEGKFTYPTGESL--VYSN 138 human
AAB94071  126 KKMFVSTGKKYNFEKGKSLCAKAGSVLASPRNEAENTALKDLIdp----sSQAYIGISDAQTEGRFMYLSGGPL--TYSN 199 chicken
NP_571645 135 QKYYVTDDVEETFDKGMQYCSSNGGALVLPRTLEENALLKVFVss---afKRLFIRITDREKEGEFVDTDRKKL--TFTN 209 zebrafish
AAH56052  151 TKIYLLVKEEKKYIDAQDYCQGRGGTLSMPKDEATNSLIASYInha--glSRVFIGINDLEREGHFVYSDRSPMq-TFNK 227 African clawed frog
NP_954705 148 SKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLaqa--glARVFIGINDLEKEGAFVYSDHSPMr-TFNK 224 human
XP_426207 426 NKIYLLVKEEKRYKEAQLYCHGRGGTLSMPKDENANNLIASYInqa--glTRVFIGINDLEKEGNFVYSDRSPMq-TFNK 502 chicken
AAH85557  151 SKVYLLVKEEKRYREAEVFCQGRGGHLAMPKDAAANRAIAGYVtda--glSRVYIGINDLEREGHFVYVERSPMt-TFSR 227 zebrafish
BAD98919  162 GKVHQLARAKLTYADARRHCRGLGGELAAPRSASDNEALRLVVpa----gEYAYIGVDDTGREGTFTYAAGGGGplGYNN 237 arctic lamprey
XP_695347 135 QKYYVTDGILGNFNDGIKFCKDAGGTLVVPKTAAENQALVRVSvssalstGKPYIGVTDRETEGQFVDIEGKQL--TFTN 212 zebrafish

Feature 1         # #     #            ##              
1B08_A    120 WAPGEPNDDggSEDCVEIF-TNGKWNDRAC-GEKRLVVCEF 158 human
1PWB_C    139 WAPGEPNDDggSEDCVEIF-TNGKWNDRAC-GEKRLVVCEF 177 human
AAB94071  200 WKPGEPNNHk-NEDCAVIE-DSGKWNDLDCsNSNIFIICEL 238 chicken
NP_571645 210 WGPNQPDNYkgAQDCGAIA-DSGLWDDVSC-DSLYPIICEI 248 zebrafish
AAH56052  228 WRQAEPNNAydEEDCAEMV-SSGGWNDVSC-LITMYFICEF 266 African clawed frog
NP_954705 225 WRSGEPNNAydEEDCVEMV-ASGGWNDVAC-HTTMYFMCEF 263 human
XP_426207 503 WRSGEPNNAydEEDCVEMV-ASGGWNDVAC-HITMYFVCEF 541 chicken
AAH85557  228 WREGEPNNAydDEDCVEMV-SSGEWIDVAC-QLTMYFVCEF 266 zebrafish
BAD98919  238 WNAGEPNNAggDEDCAVIVaNGGKWNDVRC-SRECHFVCEL 277 arctic lamprey
XP_695347 213 WGPGQPDDYrgGQDCGVIE-VSGTWDDGNC-GDIRPIICEI 251 zebrafish

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