Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/68548
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Type: Journal article
Title: Structural diversity in integrin/talin interactions
Author: Anthis, N.
Wegener, K.
Critchley, D.
Campbell, I.
Citation: Structure, 2010; 18(12):1654-1666
Publisher: Cell Press
Issue Date: 2010
ISSN: 0969-2126
1878-4186
Statement of
Responsibility: 
Nicholas J. Anthis, Kate L. Wegener, David R. Critchley, and Iain D. Campbell
Abstract: The adhesion of integrins to the extracellular matrix is regulated by binding of the cytoskeletal protein talin to the cytoplasmic tail of the β-integrin subunit. Structural studies of this interaction have hitherto largely focused on the β3-integrin, one member of the large and diverse integrin family. Here, we employ NMR to probe interactions and dynamics, revealing marked structural diversity in the contacts between β1A, β1D, and β3 tails and the Talin1 and Talin2 isoforms. Coupled with analysis of recent structures of talin/β tail complexes, these studies elucidate the thermodynamic determinants of this heterogeneity and explain why the Talin2/β1D isoforms, which are co-localized in striated muscle, form an unusually tight interaction. We also show that talin/integrin affinity can be enhanced 1000-fold by deleting two residues in the β tail. Together, these studies illustrate how the integrin/talin interaction has been fine-tuned to meet varying biological requirements.
Keywords: Humans; Talin; Protein Isoforms; Nuclear Magnetic Resonance, Biomolecular; Protein Interaction Mapping; Binding Sites; Amino Acid Sequence; Protein Structure, Secondary; Protein Structure, Tertiary; Protein Binding; Sequence Homology, Amino Acid; Models, Molecular; Mutant Proteins; Protein Interaction Domains and Motifs; Integrin beta1
Rights: Copyright 2010 Elsevier Ltd All rights reserved
RMID: 0020102928
DOI: 10.1016/j.str.2010.09.018
Description (link): http://www.cell.com/structure/home
Appears in Collections:Chemistry and Physics publications

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