7cea: Difference between revisions
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==== | ==Crystal structure of HUTS-4 Fv-clasp fragment== | ||
<StructureSection load='7cea' size='340' side='right'caption='[[7cea]]' scene=''> | <StructureSection load='7cea' size='340' side='right'caption='[[7cea]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cea]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CEA FirstGlance]. <br> | ||
</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=7cea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cea OCA], [https://pdbe.org/7cea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cea RCSB], [https://www.ebi.ac.uk/pdbsum/7cea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cea ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55Å</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=7cea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cea OCA], [https://pdbe.org/7cea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cea RCSB], [https://www.ebi.ac.uk/pdbsum/7cea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cea ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Recognition of laminin by integrin receptors is central to the epithelial cell adhesion to basement membrane, but the structural background of this molecular interaction remained elusive. Here, we report the structures of the prototypic laminin receptor alpha6beta1 integrin alone and in complex with three-chain laminin-511 fragment determined via crystallography and cryo-electron microscopy, respectively. The laminin-integrin interface is made up of several binding sites located on all five subunits, with the laminin gamma1 chain C-terminal portion providing focal interaction using two carboxylate anchor points to bridge metal-ion dependent adhesion site of integrin beta1 subunit and Asn189 of integrin alpha6 subunit. Laminin alpha5 chain also contributes to the affinity and specificity by making electrostatic interactions with large surface on the beta-propeller domain of alpha6, part of which comprises an alternatively spliced X1 region. The propeller sheet corresponding to this region shows unusually high mobility, suggesting its unique role in ligand capture. | |||
Structural mechanism of laminin recognition by integrin.,Arimori T, Miyazaki N, Mihara E, Takizawa M, Taniguchi Y, Cabanas C, Sekiguchi K, Takagi J Nat Commun. 2021 Jun 29;12(1):4012. doi: 10.1038/s41467-021-24184-8. PMID:34188035<ref>PMID:34188035</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cea" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: Arimori T]] | |||
[[Category: Takagi J]] | |||
Latest revision as of 12:22, 9 October 2024
Crystal structure of HUTS-4 Fv-clasp fragmentCrystal structure of HUTS-4 Fv-clasp fragment
Structural highlights
Publication Abstract from PubMedRecognition of laminin by integrin receptors is central to the epithelial cell adhesion to basement membrane, but the structural background of this molecular interaction remained elusive. Here, we report the structures of the prototypic laminin receptor alpha6beta1 integrin alone and in complex with three-chain laminin-511 fragment determined via crystallography and cryo-electron microscopy, respectively. The laminin-integrin interface is made up of several binding sites located on all five subunits, with the laminin gamma1 chain C-terminal portion providing focal interaction using two carboxylate anchor points to bridge metal-ion dependent adhesion site of integrin beta1 subunit and Asn189 of integrin alpha6 subunit. Laminin alpha5 chain also contributes to the affinity and specificity by making electrostatic interactions with large surface on the beta-propeller domain of alpha6, part of which comprises an alternatively spliced X1 region. The propeller sheet corresponding to this region shows unusually high mobility, suggesting its unique role in ligand capture. Structural mechanism of laminin recognition by integrin.,Arimori T, Miyazaki N, Mihara E, Takizawa M, Taniguchi Y, Cabanas C, Sekiguchi K, Takagi J Nat Commun. 2021 Jun 29;12(1):4012. doi: 10.1038/s41467-021-24184-8. PMID:34188035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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