7use

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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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3&#8491;</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=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>
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== Disease ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/CYFP1_HUMAN CYFP1_HUMAN] Angelman syndrome.
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== Publication Abstract from PubMed ==
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== Function ==
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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.
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[https://www.uniprot.org/uniprot/CYFP1_HUMAN CYFP1_HUMAN] Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA cap and mediates translational repression. In the CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E and FMR1. Promotes the translation repression activity of FMR1 in brain probably by mediating its association with EIF4E and mRNA (By similarity). Regulates formation of membrane ruffles and lamellipodia. Plays a role in axon outgrowth. Binds to F-actin but not to RNA. Part of the WAVE complex that regulates actin filament reorganization via its interaction with the Arp2/3 complex. Actin remodeling activity is regulated by RAC1. Regulator of epithelial morphogenesis. May act as an invasion suppressor in cancers.<ref>PMID:9417078</ref> <ref>PMID:16260607</ref> <ref>PMID:19524508</ref> <ref>PMID:21107423</ref>
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7use" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Rac 3D structures|Rac 3D structures]]
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*[[Wiskott-Aldrich syndrome protein 3D structures|Wiskott-Aldrich syndrome protein 3D structures]]
== References ==
== References ==
<references/>
<references/>

Current revision

Cryo-EM structure of WAVE regulatory complex with Rac1 bound on both A and D site

PDB ID 7use

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