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[[Image:2hd7.jpg|left|200px]]
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{{STRUCTURE_2hd7|  PDB=2hd7  |  SCENE=  }}
'''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]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hd7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=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>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/2hd7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hd7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Dynamic 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.


==Overview==
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<ref>PMID:17360616</ref>
Dynamic 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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2HD7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HD7 OCA].
</div>
<div class="pdbe-citations 2hd7" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17360616 17360616]
*[[Twinfilin|Twinfilin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Annila A]]
[[Category: Annila, A.]]
[[Category: Hellman MH]]
[[Category: Hellman, M H.]]
[[Category: Lappalainen P]]
[[Category: Lappalainen, P.]]
[[Category: Paavilainen VO]]
[[Category: Paavilainen, V O.]]
[[Category: Permi PI]]
[[Category: Permi, P I.]]
[[Category: Actin binding protein]]
[[Category: Adf-h]]
[[Category: Nmr]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:08:34 2008''

Latest revision as of 22:01, 29 May 2024

Solution structure of C-teminal domain of twinfilin-1.Solution structure of C-teminal domain of twinfilin-1.

Structural highlights

2hd7 is a 1 chain structure with sequence from Mus musculus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Dynamic 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 Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ Paavilainen VO, Hellman M, Helfer E, Bovellan M, Annila A, Carlier MF, Permi P, Lappalainen P. Structural basis and evolutionary origin of actin filament capping by twinfilin. Proc Natl Acad Sci U S A. 2007 Feb 27;104(9):3113-8. Epub 2007 Feb 20. PMID:17360616
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