Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor

Biochem Biophys Res Commun. 2006 Jan 6;339(1):407-14. doi: 10.1016/j.bbrc.2005.10.212. Epub 2005 Nov 14.

Abstract

The mouse betaPIX-SH3 domain, residues 8-63 of P21-activated kinase interacting exchange factor, has been characterized by X-ray diffraction. Crystals belonging to space group P3(2)21 diffracted to 2.0 A and the structure was phased by the single-wavelength anomalous diffraction method. The domain is a compact beta-barrel with an overall conformation similar to the general SH3 structure. The X-ray structure shows mouse betaPIX-SH3 domain binding the way in which the betaPIX characteristic amino acids do so for an unconventional ligand binding surface. This arrangement provides a rationale for the unusual ligand recognition motif exhibited by mouse betaPIX-SH3 domain. Comparison with another SH3/peptide complex shows that the recognition mode of the mouse betaPIX-SH3 domain should be very similar to the RXXK ligand binding mode. The unique large and planar hydrophobic pocket may contribute to the promiscuity of betaPIX-SH3 domain resulting in its multiple biological functions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Cycle Proteins / chemistry*
  • Crystallography, X-Ray
  • Dimerization
  • Guanine Nucleotide Exchange Factors / chemistry*
  • Mice
  • Models, Molecular*
  • Molecular Sequence Data
  • Rho Guanine Nucleotide Exchange Factors
  • Sequence Alignment
  • src Homology Domains*

Substances

  • Arhgef7 protein, mouse
  • Cell Cycle Proteins
  • Guanine Nucleotide Exchange Factors
  • Rho Guanine Nucleotide Exchange Factors