7ds6: Difference between revisions
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==Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (TWN-CDC)== | |||
<StructureSection load='7ds6' size='340' side='right'caption='[[7ds6]], [[Resolution|resolution]] 1.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ds6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DS6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69Å</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=7ds6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ds6 OCA], [https://pdbe.org/7ds6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ds6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ds6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ds6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CAZA1_CHICK CAZA1_CHICK] F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Twinfilin is a conserved actin regulator that interacts with actin capping protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity with the CP interaction (CPI) motif of CARMIL. Here we report the crystal structure of TWtail in complex with CP. Our structure showed that although TWtail and CARMIL CPI bind CP to an overlapping surface via their middle regions, they exhibit different CP-binding modes at both termini. Consequently, TWtail and CARMIL CPI restrict the CP in distinct conformations of open and closed forms, respectively. Interestingly, V-1, which targets CP away from the TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique CP-binding motif that regulates CP in a manner distinct from CARMIL CPI. | |||
Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail.,Takeda S, Koike R, Fujiwara I, Narita A, Miyata M, Ota M, Maeda Y J Mol Biol. 2021 Apr 30;433(9):166891. doi: 10.1016/j.jmb.2021.166891. Epub 2021 , Feb 24. PMID:33639213<ref>PMID:33639213</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Takeda | <div class="pdbe-citations 7ds6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[F-actin capping protein|F-actin capping protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Gallus gallus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Takeda S]] | |||
Latest revision as of 19:38, 29 November 2023
Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (TWN-CDC)Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (TWN-CDC)
Structural highlights
FunctionCAZA1_CHICK F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. CapZ may mediate the attachment of the barbed ends of actin filaments to the Z-line. Publication Abstract from PubMedTwinfilin is a conserved actin regulator that interacts with actin capping protein (CP) via C terminus residues (TWtail) that exhibits sequence similarity with the CP interaction (CPI) motif of CARMIL. Here we report the crystal structure of TWtail in complex with CP. Our structure showed that although TWtail and CARMIL CPI bind CP to an overlapping surface via their middle regions, they exhibit different CP-binding modes at both termini. Consequently, TWtail and CARMIL CPI restrict the CP in distinct conformations of open and closed forms, respectively. Interestingly, V-1, which targets CP away from the TWtail binding site, also favors the open-form CP. Consistently, TWtail forms a stable ternary complex with CP and V-1, a striking contrast to CARMIL CPI, which rapidly dissociates V-1 from CP. Our results demonstrate that TWtail is a unique CP-binding motif that regulates CP in a manner distinct from CARMIL CPI. Structural Insights into the Regulation of Actin Capping Protein by Twinfilin C-terminal Tail.,Takeda S, Koike R, Fujiwara I, Narita A, Miyata M, Ota M, Maeda Y J Mol Biol. 2021 Apr 30;433(9):166891. doi: 10.1016/j.jmb.2021.166891. Epub 2021 , Feb 24. PMID:33639213[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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