5xau

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==Crystal structure of integrin binding fragment of laminin-511==
==Crystal structure of integrin binding fragment of laminin-511==
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<StructureSection load='5xau' size='340' side='right' caption='[[5xau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5xau' size='340' side='right'caption='[[5xau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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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]] 1.8&#8491;</td></tr>
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<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>
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<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>
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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=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>
</table>
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== Disease ==
 
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[[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 ==
== Function ==
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[[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>
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[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5xau" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5xau" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Laminin|Laminin]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arimori, T]]
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[[Category: Homo sapiens]]
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[[Category: Kitago, Y]]
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[[Category: Large Structures]]
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[[Category: Sekiguchi, K]]
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[[Category: Arimori T]]
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[[Category: Takagi, J]]
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[[Category: Kitago Y]]
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[[Category: Takizawa, M]]
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[[Category: Sekiguchi K]]
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[[Category: Cell adhesion]]
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[[Category: Takagi J]]
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[[Category: Extracellular matrix protein]]
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[[Category: Takizawa M]]
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[[Category: Integrin]]
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[[Category: Laminin]]
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Current revision

Crystal structure of integrin binding fragment of laminin-511

PDB ID 5xau

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