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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7use]] is a 7 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=7USE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7USE FirstGlance]. <br> | <table><tr><td colspan='2'>[[7use]] is a 7 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=7USE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7USE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7use FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7use OCA], [https://pdbe.org/7use PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7use RCSB], [https://www.ebi.ac.uk/pdbsum/7use PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7use ProSAT]</span></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=7use FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7use OCA], [https://pdbe.org/7use PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7use RCSB], [https://www.ebi.ac.uk/pdbsum/7use PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7use ProSAT]</span></td></tr> | ||
</table> | </table> | ||
= | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | |||
== | The Rho-family GTPase Rac1 activates the WAVE regulatory complex (WRC) to drive Arp2/3 complex-mediated actin polymerization in many essential processes. Rac1 binds to WRC at two distinct sites-the A and D sites. Precisely how Rac1 binds and how the binding triggers WRC activation remain unknown. Here we report WRC structures by itself, and when bound to single or double Rac1 molecules, at ~3 A resolutions by cryogenic-electron microscopy. The structures reveal that Rac1 binds to the two sites by distinct mechanisms, and binding to the A site, but not the D site, drives WRC activation. Activation involves a series of unique conformational changes leading to the release of sequestered WCA (WH2-central-acidic) polypeptide, which stimulates the Arp2/3 complex to polymerize actin. Together with biochemical and cellular analyses, the structures provide a novel mechanistic understanding of how the Rac1-WRC-Arp2/3-actin signaling axis is regulated in diverse biological processes and diseases. | ||
Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase.,Ding B, Yang S, Schaks M, Liu Y, Brown AJ, Rottner K, Chowdhury S, Chen B Nat Commun. 2022 Sep 16;13(1):5444. doi: 10.1038/s41467-022-33174-3. PMID:36114192<ref>PMID:36114192</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7use" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Rac 3D structures|Rac 3D structures]] | |||
*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 08:14, 12 June 2024
Cryo-EM structure of WAVE regulatory complex with Rac1 bound on both A and D siteCryo-EM structure of WAVE regulatory complex with Rac1 bound on both A and D site
Structural highlights
Publication Abstract from PubMedThe Rho-family GTPase Rac1 activates the WAVE regulatory complex (WRC) to drive Arp2/3 complex-mediated actin polymerization in many essential processes. Rac1 binds to WRC at two distinct sites-the A and D sites. Precisely how Rac1 binds and how the binding triggers WRC activation remain unknown. Here we report WRC structures by itself, and when bound to single or double Rac1 molecules, at ~3 A resolutions by cryogenic-electron microscopy. The structures reveal that Rac1 binds to the two sites by distinct mechanisms, and binding to the A site, but not the D site, drives WRC activation. Activation involves a series of unique conformational changes leading to the release of sequestered WCA (WH2-central-acidic) polypeptide, which stimulates the Arp2/3 complex to polymerize actin. Together with biochemical and cellular analyses, the structures provide a novel mechanistic understanding of how the Rac1-WRC-Arp2/3-actin signaling axis is regulated in diverse biological processes and diseases. Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase.,Ding B, Yang S, Schaks M, Liu Y, Brown AJ, Rottner K, Chowdhury S, Chen B Nat Commun. 2022 Sep 16;13(1):5444. doi: 10.1038/s41467-022-33174-3. PMID:36114192[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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