Structural determinants of integrin recognition by talin.

Begoña García-Alvarez; José M de Pereda; David A Calderwood; Tobias S Ulmer; David Critchley; Iain D Campbell; Mark H Ginsberg; Robert C Liddington

doi:10.1016/s1097-2765(02)00823-7

PubMed · 12535520

Structural determinants of integrin recognition by talin.

Begoña García-Alvarez·José M de Pereda·David A Calderwood·Tobias S Ulmer·David Critchley·Iain D Campbell·Mark H Ginsberg·Robert C Liddington

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Abstract

The binding of cytoplasmic proteins, such as talin, to the cytoplasmic domains of integrin adhesion receptors mediates bidirectional signal transduction. Here we report the crystal structure of the principal integrin binding and activating fragment of talin, alone and in complex with fragments of the beta 3 integrin tail. The FERM (four point one, ezrin, radixin, and moesin) domain of talin engages integrins via a novel variant of the canonical phosphotyrosine binding (PTB) domain-NPxY ligand interaction that may be a prototype for FERM domain recognition of transmembrane receptors. In combination with NMR and mutational analysis, our studies reveal the critical interacting elements of both talin and the integrin beta 3 tail, providing structural paradigms for integrin linkage to the cell interior.

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Amino Acid Sequence Animals Chickens Crystallography, X-Ray Integrin beta3 Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Protein Structure, Tertiary Recombinant Fusion Proteins Sequence Alignment Signal Transduction Talin Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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Begoña García-Alvarez, José M de Pereda, David A Calderwood, Tobias S Ulmer, David Critchley, Iain D Campbell, Mark H Ginsberg, Robert C Liddington. 2003. Structural determinants of integrin recognition by talin.. https://doi.org/10.1016/s1097-2765(02)00823-7

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