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

DOI: 10.1016/j.str.2008.08.007 DOI Help
PMID: 18940607 PMID Help

Authors: Sonja Lorenz (Laboratory of Molecular Biophysics, University of Oxford,) , Ioannis Vakonakis (Laboratory of Molecular Biophysics, University of Oxford) , Iain D. Campbell (Laboratory of Molecular Biophysics, University of Oxford) , Maria K. Hoellerer (Laboratory of Molecular Biophysics, University of Oxford) , Martin E. M. Noble (Laboratory of Molecular Biophysics, University of Oxford,) , Edward D. Lowe (Laboratory of Molecular Biophysics, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Structure , VOL 8 (16) , PAGES 1521–1531

State: Published (Approved)
Published: October 2008

Abstract: The adaptor protein paxillin contains five conserved leucine-rich (LD) motifs that interact with a variety of focal adhesion proteins, such as ?-parvin. Here, we report the first crystal structure of the C-terminal calponin homology domain (CHC) of ?-parvin at 1.05 Å 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 ?-parvin-CHC, 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/?-parvin system that may facilitate the assembly of dynamic signaling complexes in the cell.

Journal Keywords: Amino; Humans; Microfilament; Models; Molecular; Paxillin; Protein; Sequence; Amino; Signal Transduction

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I04-Macromolecular Crystallography