2hd7: Difference between revisions
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==Solution structure of C-teminal domain of twinfilin-1.== | ==Solution structure of C-teminal domain of twinfilin-1.== | ||
<StructureSection load='2hd7' size='340' side='right' caption='[[2hd7]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2hd7' size='340' side='right'caption='[[2hd7]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hd7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2hd7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HD7 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ptk9 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ptk9 ([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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hd7 OCA], [https://pdbe.org/2hd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hd7 RCSB], [https://www.ebi.ac.uk/pdbsum/2hd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hd7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/TWF1_MOUSE TWF1_MOUSE]] Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.<ref>PMID:9249064</ref> <ref>PMID:10669753</ref> <ref>PMID:15282541</ref> <ref>PMID:16511569</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</div> | </div> | ||
<div class="pdbe-citations 2hd7" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2hd7" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Twinfilin|Twinfilin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Annila, A]] | [[Category: Annila, A]] | ||
Revision as of 10:36, 17 March 2021
Solution structure of C-teminal domain of twinfilin-1.Solution structure of C-teminal domain of twinfilin-1.
Structural highlights
Function[TWF1_MOUSE] Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles.[1] [2] [3] [4] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDynamic reorganization of the actin cytoskeleton is essential for motile and morphological processes in all eukaryotic cells. One highly conserved protein that regulates actin dynamics is twinfilin, which both sequesters actin monomers and caps actin filament barbed ends. Twinfilin is composed of two ADF/cofilin-like domains, Twf-N and Twf-C. Here, we reveal by systematic domain-swapping/inactivation analysis that the two functional ADF-H domains of twinfilin are required for barbed-end capping and that Twf-C plays a critical role in this process. However, these domains are not functionally equivalent. NMR-structure and mutagenesis analyses, together with biochemical and motility assays showed that Twf-C, in addition to its binding to G-actin, interacts with the sides of actin filaments like ADF/cofilins, whereas Twf-N binds only G-actin. Our results indicate that during filament barbed-end capping, Twf-N interacts with the terminal actin subunit, whereas Twf-C binds between two adjacent subunits at the side of the filament. Thus, the domain requirement for actin filament capping by twinfilin is remarkably similar to that of gelsolin family proteins, suggesting the existence of a general barbed-end capping mechanism. Furthermore, we demonstrate that a synthetic protein consisting of duplicated ADF/cofilin domains caps actin filament barbed ends, providing evidence that the barbed-end capping activity of twinfilin arose through a duplication of an ancient ADF/cofilin-like domain. Structural basis and evolutionary origin of actin filament capping by twinfilin.,Paavilainen VO, Hellman M, Helfer E, Bovellan M, Annila A, Carlier MF, Permi P, Lappalainen P Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3113-8. Epub 2007 Feb 20. PMID:17360616[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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