Conserved Protein Domain Family
Link_domain_CSPGs_modules_2_4

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cd03520: Link_domain_CSPGs_modules_2_4 
Link_domain_CSPGs_modules_2_4; this link domain is found in the second and fourth link modules of the chondroitin sulfate proteoglycan core protein (CSPG) aggrecan and, in the second link module of three other CSPGs: versican, neurocan, and brevican. The link domain is a hyaluronan (HA)-binding domain. CSPGs are characterized by an N-terminal globular domain (G1 domain) containing two contiguous link modules (modules 1 and 2). Both link modules of the G1 domain of aggrecan are involved in interaction with HA. Aggrecan in addition contains a second globular domain (G2) having link modules 3 and 4 which lack HA-binding activity. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with HA. These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggregan may contribute to the structural integrity of many different tissues. Members of the vertebrate HPLN (hyaluronan/HA and proteoglycan binding link) protein family are physically linked adjacent to CSPG genes.
Statistics
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PSSM-Id: 239597
View PSSM: cd03520
Aligned: 18 rows
Threshold Bit Score: 162.867
Threshold Setting Gi: 47214539
Created: 8-Mar-2006
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
putative
Feature 1:putative hyaluronan binding site [chemical binding site]
Evidence:
  • Comment:For CSPGs link module 2 (G1 domain) and aggrecan link module 4 (G2 domain), these two putative HA- binding sites are not well conserved.
  • Comment:HA-binding residues were identified in TSG-6 and CD44 by site-directed mutagenesis.
  • Comment:These two HA-binding residues are found at equivalent sequence positions in TSG-6 and CD44 . None of the other HA-binding residues identified were found at equivalent sequence positions in the two proteins.
  • Citation:PMID 9417085

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                ##                                                                       
gi 129886     254 EVFYAtsPEKFTFQEAANECRRLgARLATTGHVYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYVHAN 333
gi 45382043   261 KVFYAtaPGRFTLSGARRHCRGRgAALATTGQLYLAWREGLDQCDPGWLADGSVRYPILAPRRKCGGEAPGVRTLYRFPN 340
gi 118600983  261 EVFYVgpARRLTLAGARAQCRRQgAALASVGQLHLAWHEGLDQCDPGWLADGSVRYPIQTPRRRCGGPAPGVRTVYRFAN 340
gi 46048882   250 EVVHVsvPEKLTFEEAKELCRKRdGVLASVGNMYVAWRNGFDQCDYGWLADGSVRYPASVARPQCGGGLLGVRTLYRYEN 329
gi 47228553   231 EVFYPplSTKLTLQQAKDECHKHdSVIASTGQLFAAWREGLNGCDYSWLSDGSVRYPVTIPRPQCGGGLLGVRTLYKYEN 310
gi 47219432   221 VVFLDpvPQKLSFDDAQAYCRSVgAELASTAQLYLAWREGLDHCSPGWLSDGSVRYPITSPRDRCGGPRAGVRTLYRFRN 300
gi 108935831  251 DVFHItaPSKFTFEEAEAECTSRdARLATVGELQAAWRNGFDQCDYGWLSDASVRHPVTVARAQCGGGLLGVRTLYRFEN 330
gi 47214539   229 EVFHGsaPQGLTFREATAFCRSHgAEVATAAQLYAAWSDGLHRCSPGWLADGSLRYPAVTPGGRCGGAGPGVRSVYRHSN 308
gi 111306117  264 DVYYV--PEKSTLLEASNSCLRDgGMLATVGQLYSAWRKGMDQCDPGWLADNSVRYPIRNPRRNCGGEEPGVRTLYQYPN 341
gi 47226732   221 KVYYSpaKNKMSFEEARKECQKEnAVLANPGQLHAAWRLGLDRCDYGWLSDGSARHPVAVPRIQCGGGLLGVRTMYRYKN 300
                          90
                  ....*....|....*.
Feature 1                         
gi 129886     334 QTGypdpsSRYDAICY 349
gi 45382043   341 RTGfplpaSKFDAYCY 356
gi 118600983  341 RTGfpspaERFDAYCF 356
gi 46048882   330 QTGfpypdSKFDAYCY 345
gi 47228553   311 QTGfpdpaEKFGVYCF 326
gi 47219432   301 QTGfpdphSLHDVYCF 316
gi 108935831  331 QTCfplpdSRFDAYCF 346
gi 47214539   309 QTGfpeahTRHDVYCF 324
gi 111306117  342 RTGfpnptRKFGAYCF 357
gi 47226732   301 QTGfpepaTMLGAYCF 316

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