2ESW

Atomic structure of the N-terminal SH3 domain of mouse beta PIX,p21-activated kinase (PAK)-interacting exchange factor

Summary for 2ESW

• Entry DOI: 10.2210/pdb2esw/pdb
• Descriptor: Rho guanine nucleotide exchange factor 7, MERCURY (II) ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: beta barrel, sh3 domain, signaling protein
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 15255.14

Authors

Rao, Z. (deposition date: 2005-10-27, release date: 2006-04-11, Last modification date: 2024-03-13)

Primary citation

Li, X.,Liu, X.,Sun, F.,Gao, J.,Zhou, H.,Gao, G.F.,Bartlam, M.,Rao, Z.
Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-activated kinase-interacting exchange factor
Biochem.Biophys.Res.Commun., 339:407-414, 2006

PubMed 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.

PubMed: 16307729
DOI: 10.1016/j.bbrc.2005.10.212

Experimental method

X-RAY DIFFRACTION (2.01 Å)