We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2hd7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hd7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hd7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hd7| PDB=2hd7 | SCENE= }}
{{STRUCTURE_2hd7| PDB=2hd7 | SCENE= }}
-
'''Solution structure of C-teminal domain of twinfilin-1.'''
+
===Solution structure of C-teminal domain of twinfilin-1.===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17360616}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17360616 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17360616}}
==About this Structure==
==About this Structure==
-
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].
+
2HD7 is a [[Single protein]] structure of sequence from [http://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].
==Reference==
==Reference==
Line 30: Line 34:
[[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 Jul 28 13:10:16 2008''

Revision as of 10:10, 28 July 2008

Image:2hd7.png

Template:STRUCTURE 2hd7

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

Template:ABSTRACT PUBMED 17360616

About this Structure

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

Reference

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 Mon Jul 28 13:10:16 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hd7"
Personal tools