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.
Statistics
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PSSM-Id: 153061
View PSSM: cd03591
Aligned: 23 rows
Threshold Bit Score: 175.177
Threshold Setting Gi: 66472052
Created: 21-Mar-2006
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
 
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
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  • Structure:1KWY_A, rat mannose protein A trimer bound with Man-A13-Man, contacts at 3.5 A.
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  • Structure:1KX1_F, rat Mannose Protein A bound with Man6-Glcnac2-Asn and calcium ion, contacts at 3.5 A.
    View structure with Cn3D
  • 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
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  • 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
    View structure with Cn3D
  • 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.
    View structure with Cn3D
  • 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.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                       
1B08_A       45 EKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVva---knEAAFLSMTDSKTEGKFTYPTGESL--VYSN 119
1PWB_C       64 EKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVva---knEAAFLSMTDSKTEGKFTYPTGESL--VYSN 138
gi 2736145  126 KKMFVSTGKKYNFEKGKSLCAKAGSVLASPRNEAENTALKDLIdp----sSQAYIGISDAQTEGRFMYLSGGPL--TYSN 199
gi 18858997 135 QKYYVTDDVEETFDKGMQYCSSNGGALVLPRTLEENALLKVFVss---afKRLFIRITDREKEGEFVDTDRKKL--TFTN 209
gi 33417124 151 TKIYLLVKEEKKYIDAQDYCQGRGGTLSMPKDEATNSLIASYInha--glSRVFIGINDLEREGHFVYSDRSPMq-TFNK 227
gi 40548420 148 SKIYLLVKEEKRYADAQLSCQGRGGTLSMPKDEAANGLMAAYLaqa--glARVFIGINDLEKEGAFVYSDHSPMr-TFNK 224
gi 50744990 426 NKIYLLVKEEKRYKEAQLYCHGRGGTLSMPKDENANNLIASYInqa--glTRVFIGINDLEKEGNFVYSDRSPMq-TFNK 502
gi 55250116 151 SKVYLLVKEEKRYREAEVFCQGRGGHLAMPKDAAANRAIAGYVtda--glSRVYIGINDLEREGHFVYVERSPMt-TFSR 227
gi 66472052 162 GKVHQLARAKLTYADARRHCRGLGGELAAPRSASDNEALRLVVpa----gEYAYIGVDDTGREGTFTYAAGGGGplGYNN 237
gi 68356570 135 QKYYVTDGILGNFNDGIKFCKDAGGTLVVPKTAAENQALVRVSvssalstGKPYIGVTDRETEGQFVDIEGKQL--TFTN 212
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
Feature 1           # #     #            ##              
1B08_A      120 WAPGEPNDDggSEDCVEIF-TNGKWNDRAC-GEKRLVVCEF 158
1PWB_C      139 WAPGEPNDDggSEDCVEIF-TNGKWNDRAC-GEKRLVVCEF 177
gi 2736145  200 WKPGEPNNHk-NEDCAVIE-DSGKWNDLDCsNSNIFIICEL 238
gi 18858997 210 WGPNQPDNYkgAQDCGAIA-DSGLWDDVSC-DSLYPIICEI 248
gi 33417124 228 WRQAEPNNAydEEDCAEMV-SSGGWNDVSC-LITMYFICEF 266
gi 40548420 225 WRSGEPNNAydEEDCVEMV-ASGGWNDVAC-HTTMYFMCEF 263
gi 50744990 503 WRSGEPNNAydEEDCVEMV-ASGGWNDVAC-HITMYFVCEF 541
gi 55250116 228 WREGEPNNAydDEDCVEMV-SSGEWIDVAC-QLTMYFVCEF 266
gi 66472052 238 WNAGEPNNAggDEDCAVIVaNGGKWNDVRC-SRECHFVCEL 277
gi 68356570 213 WGPGQPDDYrgGQDCGVIE-VSGTWDDGNC-GDIRPIICEI 251

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