6rsq
From Proteopedia
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<StructureSection load='6rsq' size='340' side='right'caption='[[6rsq]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='6rsq' size='340' side='right'caption='[[6rsq]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6rsq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RSQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RSQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6rsq]] is a 4 chain structure with sequence from [http://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=6RSQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RSQ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cap1, Cap ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rsq OCA], [http://pdbe.org/6rsq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rsq RCSB], [http://www.ebi.ac.uk/pdbsum/6rsq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rsq ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rsq OCA], [http://pdbe.org/6rsq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rsq RCSB], [http://www.ebi.ac.uk/pdbsum/6rsq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rsq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CAP1_MOUSE CAP1_MOUSE]] Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. | [[http://www.uniprot.org/uniprot/CAP1_MOUSE CAP1_MOUSE]] Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The ability of cells to generate forces through actin filament turnover was an early adaptation in evolution. While much is known about how actin filaments grow, mechanisms of their disassembly are incompletely understood. The best-characterized actin disassembly factors are the cofilin family proteins, which increase cytoskeletal dynamics by severing actin filaments. However, the mechanism by which severed actin filaments are recycled back to monomeric form has remained enigmatic. We report that cyclase-associated-protein (CAP) works in synergy with cofilin to accelerate actin filament depolymerization by nearly 100-fold. Structural work uncovers the molecular mechanism by which CAP interacts with actin filament pointed end to destabilize the interface between terminal actin subunits, and subsequently recycles the newly-depolymerized actin monomer for the next round of filament assembly. These findings establish CAP as a molecular machine promoting rapid actin filament depolymerization and monomer recycling, and explain why CAP is critical for actin-dependent processes in all eukaryotes. | ||
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| + | Mechanism of synergistic actin filament pointed end depolymerization by cyclase-associated protein and cofilin.,Kotila T, Wioland H, Enkavi G, Kogan K, Vattulainen I, Jegou A, Romet-Lemonne G, Lappalainen P Nat Commun. 2019 Nov 22;10(1):5320. doi: 10.1038/s41467-019-13213-2. PMID:31757941<ref>PMID:31757941</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6rsq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Kogan, K]] | [[Category: Kogan, K]] | ||
[[Category: Kotila, T]] | [[Category: Kotila, T]] | ||
Revision as of 10:54, 4 December 2019
Helical folded domain of mouse CAP1
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