Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/26740
Title: The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.
Authors: Kalli, AC
Wegener, KL
Goult, BT
Anthis, NJ
Campbell, ID
Sansom, MS
First Published: 13-Oct-2010
Citation: STRUCTURE, 2010, 18 (10), pp. 1280-1288
Abstract: Integrins are cell surface receptors crucial for cell migration and adhesion. They are activated by interactions of the talin head domain with the membrane surface and the integrin β cytoplasmic tail. Here, we use coarse-grained molecular dynamic simulations and nuclear magnetic resonance spectroscopy to elucidate the membrane-binding surfaces of the talin head (F2-F3) domain. In particular, we show that mutations in the four basic residues (K258E, K274E, R276E, and K280E) in the F2 binding surface reduce the affinity of the F2-F3 for the membrane and modify its orientation relative to the bilayer. Our results highlight the key role of anionic lipids in talin/membrane interactions. Simulation of the F2-F3 in complex with the α/β transmembrane dimer reveals information for its orientation relative to the membrane. Our studies suggest that the perturbed orientation of talin relative to the membrane in the F2 mutant would be expected to in turn perturb talin/integrin interactions.
DOI Link: 10.1016/j.str.2010.07.012
eISSN: 1878-4186
Links: http://hdl.handle.net/2381/26740
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.