7ajl
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==Cyrstal structure of CYRI-B/Fam49B== | ==Cyrstal structure of CYRI-B/Fam49B== | ||
| - | <StructureSection load='7ajl' size='340' side='right'caption='[[7ajl]]' scene=''> | + | <StructureSection load='7ajl' size='340' side='right'caption='[[7ajl]], [[Resolution|resolution]] 2.37Å' 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=7AJL OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[7ajl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AJL FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cyrib, Cyri, Fam49b ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=7ajl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ajl OCA], [https://pdbe.org/7ajl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ajl RCSB], [https://www.ebi.ac.uk/pdbsum/7ajl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ajl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/CYRIB_MOUSE CYRIB_MOUSE]] Negatively regulates RAC1 signaling and RAC1-driven cytoskeletal remodeling (PubMed:31285585). Regulates chemotaxis, cell migration and epithelial polarization by controlling the polarity, plasticity, duration and extent of protrusions. Limits Rac1 mediated activation of the Scar/WAVE complex, focuses protrusion signals and regulates pseudopod complexity by inhibiting Scar/WAVE-induced actin polymerization (By similarity). Protects against Salmonella bacterial infection. Attenuates processes such as macropinocytosis, phagocytosis and cell migration and restrict sopE-mediated bacterial entry (PubMed:31285585). Restricts also infection mediated by Mycobacterium tuberculosis and Listeria monocytogenes (PubMed:31285585). Involved in the regulation of mitochondrial dynamics and oxidative stress (PubMed:29059164).[UniProtKB:Q9NUQ9]<ref>PMID:29059164</ref> <ref>PMID:31285585</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rac1 is a major regulator of actin dynamics, with GTP-bound Rac1 promoting actin assembly via the Scar/WAVE complex. CYRI competes with Scar/WAVE for interaction with Rac1 in a feedback loop regulating actin dynamics. Here, we reveal the nature of the CYRI-Rac1 interaction, through crystal structures of CYRI-B lacking the N-terminal helix (CYRI-BDeltaN) and the CYRI-BDeltaN:Rac1Q61L complex, providing the molecular basis for CYRI-B regulation of the Scar/WAVE complex. We reveal CYRI-B as having two subdomains - an N-terminal Rac1 binding subdomain with a unique Rac1-effector interface and a C-terminal Ratchet subdomain that undergoes conformational changes induced by Rac1 binding. Finally, we show that the CYRI protein family, CYRI-A and CYRI-B can produce an autoinhibited hetero- or homodimers, adding an additional layer of regulation to Rac1 signaling. | ||
| + | |||
| + | Structural Basis of CYRI-B Direct Competition with Scar/WAVE Complex for Rac1.,Yelland T, Le AH, Nikolaou S, Insall R, Machesky L, Ismail S Structure. 2021 Mar 4;29(3):226-237.e4. doi: 10.1016/j.str.2020.11.003. Epub 2020, Nov 19. PMID:33217330<ref>PMID:33217330</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7ajl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Anh H]] | + | [[Category: Lk3 transgenic mice]] |
| - | [[Category: Insall R]] | + | [[Category: Anh, H]] |
| - | [[Category: Ismail S]] | + | [[Category: Insall, R]] |
| - | [[Category: Machesky L]] | + | [[Category: Ismail, S]] |
| - | [[Category: Yelland T]] | + | [[Category: Machesky, L]] |
| + | [[Category: Yelland, T]] | ||
| + | [[Category: Actin regulation]] | ||
| + | [[Category: Cytosolic protein]] | ||
| + | [[Category: Rac1 competitor]] | ||
| + | [[Category: Scar/wave inhibitor]] | ||
Revision as of 14:48, 2 June 2021
Cyrstal structure of CYRI-B/Fam49B
| |||||||||||
