Please use this identifier to cite or link to this item:
Title: The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site.
Authors: Goult, BT
Gingras, AR
Bate, N
Barsukov, IL
Critchley, DR
Roberts, GC
First Published: 3-Jun-2010
Citation: FEBS LETT, 2010, 584 (11), pp. 2237-2241
Abstract: Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.
DOI Link: 10.1016/j.febslet.2010.04.028
eISSN: 1873-3468
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
There are no files associated with this item.

Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.