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Structural Analysis of the Interactions Between Paxillin LD Motifs and α-Parvin

Lookup NU author(s): Professor Martin Noble

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Abstract

The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as alpha-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CH(C)) of alpha-parvin at 1.05 A resolution and show that it is able to bind all the LD motifs, with some selectivity for LD1, LD2, and LD4. Cocrystal structures with these LD motifs reveal the molecular details of their interactions with a common binding site on alpha-parvin-CH(C), which is located at the rim of the canonical fold and includes part of the inter-CH domain linker. Surprisingly, this binding site can accommodate LD motifs in two antiparallel orientations. Taken together, these results reveal an unusual degree of binding degeneracy in the paxillin/alpha-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.


Publication metadata

Author(s): Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble MEM, Hoellerer MK

Publication type: Article

Publication status: Published

Journal: Structure

Year: 2008

Volume: 16

Issue: 10

Pages: 1521-1531

ISSN (print): 0969-2126

ISSN (electronic): 1878-4186

Publisher: Cell Press

URL: http://dx.doi.org/10.1016/j.str.2008.08.007

DOI: 10.1016/j.str.2008.08.007

PubMed id: 2572193


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