5xau
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | The entry | + | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XAU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xau OCA], [http://pdbe.org/5xau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xau RCSB], [http://www.ebi.ac.uk/pdbsum/5xau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xau ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/LAMB1_HUMAN LAMB1_HUMAN]] Cobblestone lissencephaly without muscular or ocular involvement. The disease is caused by mutations affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [[http://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. [[http://www.uniprot.org/uniprot/LAMC1_HUMAN LAMC1_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. [[http://www.uniprot.org/uniprot/LAMB1_HUMAN LAMB1_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. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.<ref>PMID:23472759</ref> | ||
| + | <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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arimori, T]] | ||
| + | [[Category: Kitago, Y]] | ||
| + | [[Category: Sekiguchi, K]] | ||
| + | [[Category: Takagi, J]] | ||
| + | [[Category: Takizawa, M]] | ||
| + | [[Category: Cell adhesion]] | ||
| + | [[Category: Extracellular matrix protein]] | ||
| + | [[Category: Integrin]] | ||
| + | [[Category: Laminin]] | ||
Revision as of 04:29, 21 September 2017
Crystal structure of integrin binding fragment of laminin-511
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