2VZI

Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD4 motif

Summary for 2VZI

• Entry DOI: 10.2210/pdb2vzi/pdb
• Related: 1KKY 1KL0 2VZC 2VZD 2VZG
• Descriptor: Paxillin,Paxillin, Alpha-parvin, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• Functional Keywords: cell adhesion, cell membrane, metal-binding, calponin homology domain, cytoskeleton, cell junction, actin-binding, membrane, ld2 motif, lim domain, phosphoprotein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 18079.71

Authors

Lorenz, S.,Vakonakis, I.,Lowe, E.D.,Campbell, I.D.,Noble, M.E.M.,Hoellerer, M.K. (deposition date: 2008-08-01, release date: 2008-10-28, Last modification date: 2023-12-13)

Primary citation

Lorenz, S.,Vakonakis, I.,Lowe, E.D.,Campbell, I.D.,Noble, M.E.,Hoellerer, M.K.
Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.
Structure, 16:1521-1531, 2008

PubMed 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.

PubMed: 18940607
DOI: 10.1016/j.str.2008.08.007

Experimental method

X-RAY DIFFRACTION (2.2 Å)