2hd7: Difference between revisions

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[[Image:2hd7.jpg|left|200px]]
[[Image:2hd7.jpg|left|200px]]


{{Structure
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|GENE= Ptk9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
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{{STRUCTURE_2hd7| PDB=2hd7 |  SCENE= }}  
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hd7 OCA], [http://www.ebi.ac.uk/pdbsum/2hd7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hd7 RCSB]</span>
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'''Solution structure of C-teminal domain of twinfilin-1.'''
'''Solution structure of C-teminal domain of twinfilin-1.'''
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[[Category: Paavilainen, V O.]]
[[Category: Paavilainen, V O.]]
[[Category: Permi, P I.]]
[[Category: Permi, P I.]]
[[Category: actin binding protein]]
[[Category: Actin binding protein]]
[[Category: adf-h]]
[[Category: Adf-h]]
[[Category: nmr]]
[[Category: Nmr]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:08:34 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:28:42 2008''

Revision as of 06:08, 4 May 2008

File:2hd7.jpg

Template:STRUCTURE 2hd7

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


OverviewOverview

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 StructureAbout this Structure

2HD7 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

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 Page seeded by OCA on Sun May 4 06:08:34 2008

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