5mx1
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human chondroadherin== | |
| + | <StructureSection load='5mx1' size='340' side='right' caption='[[5mx1]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mx1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MX1 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5mx1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mx1 OCA], [http://pdbe.org/5mx1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mx1 RCSB], [http://www.ebi.ac.uk/pdbsum/5mx1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mx1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/CHAD_HUMAN CHAD_HUMAN]] Promotes attachment of chondrocytes, fibroblasts, and osteoblasts. This binding is mediated (at least for chondrocytes and fibroblasts) by the integrin alpha(2)beta(1). May play an important role in the regulation of chondrocyte growth and proliferation (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The small leucine-rich proteoglycans (SLRPs) are important regulators of extracellular matrix assembly and cell signalling. We have determined crystal structures at ~2.2A resolution of human fibromodulin and chondroadherin, two collagen-binding SLRPs. Their overall fold is similar to that of the prototypical SLRP, decorin, but unlike decorin neither fibromodulin nor chondroadherin forms a stable dimer. A previously identified binding site for integrin alpha2beta1 maps to an alpha-helix in the C-terminal cap region of chondroadherin. Interrogation of the Collagen Toolkits revealed a unique binding site for chondroadherin in collagen II, and no binding to collagen III. A triple-helical peptide containing the sequence GAOGPSGFQGLOGPOGPO (O is hydroxyproline) forms a stable complex with chondroadherin in solution. In fibrillar collagen I and II, this sequence is aligned with the collagen cross-linking site KGHR, suggesting a role for chondroadherin in cross-linking. | ||
| - | + | Structural and functional analysis of two small leucine-rich repeat proteoglycans, fibromodulin and chondroadherin.,Paracuellos P, Kalamajski S, Bonna A, Bihan D, Farndale RW, Hohenester E Matrix Biol. 2017 Feb 17. pii: S0945-053X(17)30015-X. doi:, 10.1016/j.matbio.2017.02.002. PMID:28215822<ref>PMID:28215822</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5mx1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Hohenester, E]] | ||
| + | [[Category: Paracuellos, P]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Collagen binding]] | ||
| + | [[Category: Extracellular matrix]] | ||
| + | [[Category: Leucine-rich repeat]] | ||
Revision as of 09:38, 11 March 2017
Crystal structure of human chondroadherin
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