Crystal Structure of the N-terminal Sh3 Domain of Mouse Betapix, P21-activated Kinase-interacting Exchange Factor.
From: Laboratory of Structural Biology, Tsinghua University, Beijing 100084, China.
Biochemical and biophysical research communications
- Publish Date: Jan 2006
- ISSN: 0006-291X
- Volume: 339
- Issue: 1
- Pages: 407-14
- Medium: Print
- Language: English
- Citation (JAMA): Li Xiaofeng, Liu Xueqi, Sun Fei, et al. Crystal Structure of the N-terminal Sh3 Domain of Mouse Betapix, P21-activated Kinase-interacting Exchange Factor.. Biochem. Biophys. Res. Commun. Jan 2006;339:407-14
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.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Binding Sites, Cell Cycle Proteins, Crystallography, X-Ray, Dimerization, Guanine Nucleotide Exchange Factors, Mice, Models, Molecular, Molecular Sequence Data, Sequence Alignment, src Homology Domains
Check for Full Text / PubMed Unique Identifier (PMID): 16307729
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