5xau
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of integrin binding fragment of laminin-511== | |
| + | <StructureSection load='5xau' size='340' side='right'caption='[[5xau]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5xau]] is a 6 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=5XAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XAU 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]] 1.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5xau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xau OCA], [https://pdbe.org/5xau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xau RCSB], [https://www.ebi.ac.uk/pdbsum/5xau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xau ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LAMA5_HUMAN LAMA5_HUMAN] Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins-three laminin globular domains of the alpha chain (LG1-3) and the carboxyl-terminal tail of the gamma chain (gamma-tail)-are required for integrin binding, but it remains unclear how the gamma-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the gamma-tail extends to the bottom face of LG1-3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1-3 with the gamma1-tail apposed to the metal ion-dependent adhesion site (MIDAS) of integrin beta1. These findings are consistent with a model in which the gamma-tail coordinates the metal ion in the MIDAS through its Glu residue. | ||
| - | + | Mechanistic basis for the recognition of laminin-511 by alpha6beta1 integrin.,Takizawa M, Arimori T, Taniguchi Y, Kitago Y, Yamashita E, Takagi J, Sekiguchi K Sci Adv. 2017 Sep 1;3(9):e1701497. doi: 10.1126/sciadv.1701497. eCollection 2017 , Sep. PMID:28879238<ref>PMID:28879238</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5xau" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Laminin|Laminin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Arimori T]] | ||
| + | [[Category: Kitago Y]] | ||
| + | [[Category: Sekiguchi K]] | ||
| + | [[Category: Takagi J]] | ||
| + | [[Category: Takizawa M]] | ||
Current revision
Crystal structure of integrin binding fragment of laminin-511
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