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2d8b

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Revision as of 11:55, 3 February 2021

Solution structure of the second tandem cofilin-domain of mouse twinfilin

Structural highlights

2d8b is a 1 chain structure with sequence from Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Ptk9 (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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 PubMed

Actin is one of the most conserved proteins in nature. Its assembly and disassembly are regulated by many proteins, including the family of actin-depolymerizing factor homology (ADF-H) domains. ADF-H domains can be divided into five classes: ADF/cofilin, glia maturation factor (GMF), coactosin, twinfilin, and Abp1/drebrin. The best-characterized class is ADF/cofilin. The other four classes have drawn much less attention and very few structures have been reported. This study presents the solution NMR structure of the ADF-H domain of human HIP-55-drebrin-like protein, the first published structure of a drebrin-like domain (mammalian), and the first published structure of GMF beta (mouse). We also determined the structures of mouse GMF gamma, the mouse coactosin-like domain and the C-terminal ADF-H domain of mouse twinfilin 1. Although the overall fold of the five domains is similar, some significant differences provide valuable insights into filamentous actin (F-actin) and globular actin (G-actin) binding, including the identification of binding residues on the long central helix. This long helix is stabilized by three or four residues. Notably, the F-actin binding sites of mouse GMF beta and GMF gamma contain two additional beta-strands not seen in other ADF-H structures. The G-actin binding site of the ADF-H domain of human HIP-55-drebrin-like protein is absent and distorted in mouse GMF beta and GMF gamma.

NMR solution structures of actin depolymerizing factor homology domains.,Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Beeler JF, Patel BK, Chedid M, LaRochelle WJ. Cloning and characterization of the mouse homolog of the human A6 gene. Gene. 1997 Jul 1;193(1):31-7. PMID:9249064
↑ Vartiainen M, Ojala PJ, Auvinen P, Peranen J, Lappalainen P. Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics. Mol Cell Biol. 2000 Mar;20(5):1772-83. PMID:10669753
↑ Falck S, Paavilainen VO, Wear MA, Grossmann JG, Cooper JA, Lappalainen P. Biological role and structural mechanism of twinfilin-capping protein interaction. EMBO J. 2004 Aug 4;23(15):3010-9. Epub 2004 Jul 29. PMID:15282541 doi:http://dx.doi.org/10.1038/sj.emboj.7600310
↑ Helfer E, Nevalainen EM, Naumanen P, Romero S, Didry D, Pantaloni D, Lappalainen P, Carlier MF. Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility. EMBO J. 2006 Mar 22;25(6):1184-95. Epub 2006 Mar 2. PMID:16511569 doi:http://dx.doi.org/7601019
↑ Goroncy AK, Koshiba S, Tochio N, Tomizawa T, Sato M, Inoue M, Watanabe S, Hayashizaki Y, Tanaka A, Kigawa T, Yokoyama S. NMR solution structures of actin depolymerizing factor homology domains. Protein Sci. 2009 Nov;18(11):2384-92. PMID:19768801 doi:10.1002/pro.248

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2d8b"

@@ Line 1: / Line 1: @@
 ==Solution structure of the second tandem cofilin-domain of mouse twinfilin==
-<StructureSection load='2d8b' size='340' side='right' caption='[[2d8b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2d8b' size='340' side='right'caption='[[2d8b]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d8b]] is a 1 chain structure with sequence from [http://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=2D8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2D8B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d8b]] 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=2D8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D8B FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Ptk9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d8b OCA], [http://pdbe.org/2d8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d8b RCSB], [http://www.ebi.ac.uk/pdbsum/2d8b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d8b ProSAT], [http://www.topsan.org/Proteins/RSGI/2d8b TOPSAN]</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=2d8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d8b OCA], [https://pdbe.org/2d8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d8b RCSB], [https://www.ebi.ac.uk/pdbsum/2d8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d8b ProSAT], [https://www.topsan.org/Proteins/RSGI/2d8b TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 </div>
 <div class="pdbe-citations 2d8b" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Twinfilin|Twinfilin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Lk3 transgenic mice]]
 [[Category: Goroncy, A K]]

2d8b

From Proteopedia

Revision as of 11:55, 3 February 2021

Solution structure of the second tandem cofilin-domain of mouse twinfilin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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