5yq5

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'''Unreleased structure'''
 
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The entry 5yq5 is ON HOLD
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==Crystal structure of human osteomodulin==
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<StructureSection load='5yq5' size='340' side='right'caption='[[5yq5]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yq5]] is a 4 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=5YQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YQ5 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yq5 OCA], [https://pdbe.org/5yq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yq5 RCSB], [https://www.ebi.ac.uk/pdbsum/5yq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yq5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OMD_HUMAN OMD_HUMAN] May be implicated in biomineralization processes. Has a function in binding of osteoblasts via the alpha(V)beta(3)-integrin (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Small leucine-rich repeat proteoglycan (SLRP) proteins have an important role in the organization of the extracellular matrix, especially in the formation of collagen fibrils. However, the mechanism governing the shape of collagen fibrils is poorly understood. Here, we report that the protein Osteomodulin (OMD) of the SLRP family is a monomeric protein in solution that interacts with type-I collagen. This interaction is dominated by weak electrostatic forces employing negatively charged residues of OMD, in particular Glu284 and Glu303, and controlled by entropic factors. The protein OMD establishes a fast-binding equilibrium with collagen, where OMD may engage not only with individual collagen molecules, but also with the growing fibrils. This weak electrostatic interaction is carefully balanced so it modulates the shape of the fibrils without compromising their viability.
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Authors:
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Molecular basis for governing the morphology of type-I collagen fibrils by Osteomodulin.,Tashima T, Nagatoishi S, Caaveiro JMM, Nakakido M, Sagara H, Kusano-Arai O, Iwanari H, Mimuro H, Hamakubo T, Ohnuma SI, Tsumoto K Commun Biol. 2018 Apr 19;1:33. doi: 10.1038/s42003-018-0038-2. eCollection 2018. PMID:30271919<ref>PMID:30271919</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5yq5" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Caaveiro JMM]]
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[[Category: Tashima T]]
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[[Category: Tsumoto K]]

Current revision

Crystal structure of human osteomodulin

PDB ID 5yq5

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