2VZI: Crystal Structure Of The C-Terminal Calponin Homology Domain Of Alpha-Parvin In Complex With Paxillin Ld4 Motif

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.
PDB ID: 2VZIDownload
MMDB ID: 67589
PDB Deposition Date: 2008/8/1
Updated in MMDB: 2008/10
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Source Organism:
Similar Structures:
Biological Unit for 2VZI: dimeric; determined by author and by software (PQS)
Molecular Components in 2VZI
Label Count Molecule
Proteins (2 molecules)
Paxillin(Gene symbol: PXN)
Molecule annotation
Alpha-parvin(Gene symbol: PARVA)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB