Browse by author
Lookup NU author(s): Professor Martin Noble
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
Author(s): Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble MEM, Hoellerer MK
Publication type: Article
Publication status: Published
ISSN (print): 0969-2126
ISSN (electronic): 1878-4186
Publisher: Cell Press
PubMed id: 2572193
Altmetrics provided by Altmetric