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https://hdl.handle.net/2440/88460
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Type: | Journal article |
Title: | The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study |
Author: | Kalli, A. Wegener, K. Goult, B. Anthis, N. Campbell, I. Sansom, M. |
Citation: | Structure, 2010; 18(10):1280-1288 |
Publisher: | Elsevier |
Issue Date: | 2010 |
ISSN: | 0969-2126 1878-4186 |
Statement of Responsibility: | Antreas C. Kalli, Kate L. Wegener, Benjamin T. Goult, Nicholas J. Anthis, Iain D. Campbell, and Mark S.P. Sansom |
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. |
Keywords: | Animals Humans Multiprotein Complexes Membrane Lipids Lipid Bilayers Talin Magnetic Resonance Spectroscopy Protein Structure, Tertiary Protein Binding Sequence Homology, Amino Acid Mutation Binding Sites Amino Acid Sequence Molecular Sequence Data Platelet Membrane Glycoprotein IIb Molecular Dynamics Simulation Protein Multimerization Antigens, CD29 Models, Molecular |
Rights: | © 2010 Elsevier Ltd All rights reserved |
DOI: | 10.1016/j.str.2010.07.012 |
Published version: | http://dx.doi.org/10.1016/j.str.2010.07.012 |
Appears in Collections: | Aurora harvest 2 Molecular and Biomedical Science publications |
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