7nxd: Difference between revisions
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==== | ==Cryo-EM structure of human integrin alpha5beta1 in the half-bent conformation== | ||
<StructureSection load='7nxd' size='340' side='right'caption='[[7nxd]]' scene=''> | <StructureSection load='7nxd' size='340' side='right'caption='[[7nxd]], [[Resolution|resolution]] 4.60Å' 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'>[[7nxd]] is a 2 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=7NXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NXD 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=7nxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nxd OCA], [https://pdbe.org/7nxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nxd RCSB], [https://www.ebi.ac.uk/pdbsum/7nxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nxd ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7nxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nxd OCA], [https://pdbe.org/7nxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nxd RCSB], [https://www.ebi.ac.uk/pdbsum/7nxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nxd ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ITA5_HUMAN ITA5_HUMAN] Integrin alpha-5/beta-1 is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. In case of HIV-1 infection, the interaction with extracellular viral Tat protein seems to enhance angiogenesis in Kaposi's sarcoma lesions. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Integrin alpha(5)beta(1) is a major fibronectin receptor critical for cell migration. Upon complex formation, fibronectin and alpha(5)beta(1) undergo conformational changes. While this is key for cell-tissue connections, its mechanism is unknown. Here, we report cryo-electron microscopy structures of native human alpha(5)beta(1) with fibronectin to 3.1-angstrom resolution, and in its resting state to 4.6-angstrom resolution. The alpha(5)beta(1)-fibronectin complex revealed simultaneous interactions at the arginine-glycine-aspartate loop, the synergy site, and a newly identified binding site proximal to adjacent to metal ion-dependent adhesion site, inducing the translocation of helix alpha1 to secure integrin opening. Resting alpha(5)beta(1) adopts an incompletely bent conformation, challenging the model of integrin sharp bending inhibiting ligand binding. Our biochemical and structural analyses showed that affinity of alpha(5)beta(1) for fibronectin is increased with manganese ions (Mn(2+)) while adopting the half-bent conformation, indicating that ligand-binding affinity does not depend on conformation, and alpha(5)beta(1) opening is induced by ligand-binding. | |||
Structural insights into integrin alpha(5)beta(1) opening by fibronectin ligand.,Schumacher S, Dedden D, Nunez RV, Matoba K, Takagi J, Biertumpfel C, Mizuno N Sci Adv. 2021 May 7;7(19):eabe9716. doi: 10.1126/sciadv.abe9716. Print 2021 May. PMID:33962943<ref>PMID:33962943</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7nxd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Integrin 3D structures|Integrin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Biertumpfel C]] | ||
[[Category: Dedden D]] | |||
[[Category: Matoba K]] | |||
[[Category: Mizuno N]] | |||
[[Category: Schumacher S]] | |||
[[Category: Takagi J]] | |||
[[Category: Vazquez Nunez R]] | |||