5mx0: Difference between revisions
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New page: '''Unreleased structure''' The entry 5mx0 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Crystal structure of human fibromodulin== | ||
<StructureSection load='5mx0' size='340' side='right'caption='[[5mx0]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mx0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MX0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5mx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mx0 OCA], [https://pdbe.org/5mx0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mx0 RCSB], [https://www.ebi.ac.uk/pdbsum/5mx0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mx0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FMOD_HUMAN FMOD_HUMAN] Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (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 5mx0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hohenester E]] | |||
[[Category: Paracuellos P]] | |||
Latest revision as of 17:52, 8 November 2023
Crystal structure of human fibromodulin
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