5lfn
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of human chondroadherin== | |
| + | <StructureSection load='5lfn' size='340' side='right' caption='[[5lfn]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5lfn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LFN 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></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=5lfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfn OCA], [http://pdbe.org/5lfn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lfn RCSB], [http://www.ebi.ac.uk/pdbsum/5lfn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfn 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 == | ||
| + | Chondroadherin is a cartilage matrix protein that is known to mediate the adhesion of isolated chondrocytes. Its protein core is composed of 11 leucine-rich repeats flanked by cysteine-rich domains at the N- and C-terminal ends. Recombinant human chondroadherin was crystallized using the sitting-drop vapour-diffusion method. The crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 56.4, b = 111.3, c = 128.5 A, beta = 92.2, and are most likely to contain four molecules in the asymmetric unit. The crystals diffracted to at least 2.3 A using synchrotron radiation, but structure determination using molecular replacement has so far been unsuccessful. | ||
| - | + | Purification, crystallization and preliminary X-ray diffraction analysis of human chondroadherin.,Pramhed A, Addis L, Tillgren V, Wenglen C, Heinegard D, Logan DT Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):516-9. doi:, 10.1107/S1744309108012141. Epub 2008 May 23. PMID:18540064<ref>PMID:18540064</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5lfn" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: LOGAN, D T]] | ||
| + | [[Category: PRAMHED, A]] | ||
| + | [[Category: RAMISCH, S]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Chondroadherin]] | ||
| + | [[Category: Extracellular matrix]] | ||
| + | [[Category: Small leucine-rich repeat protein]] | ||
Revision as of 16:15, 2 January 2017
Crystal structure of human chondroadherin
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