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

被引：8
作者：
Li, XF
Liu, XQ
Sun, F
Gao, J
Zhou, HW
Gao, GF
Bartlam, M
Rao, ZH [1 ]
机构：
[1] Tsinghua Univ, Lab Struct Biol, Beijing 100084, Peoples R China
[2] Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
[3] Chinese Acad Sci, Inst Microbiol, Ctr Mol Immunol, Beijing 100080, Peoples R China
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2006年 / 339卷 / 01期
基金：
中国国家自然科学基金;
关键词：
beta PIX; SH3; domain; crystal structure; ligand; binding pocket;
D O I：
10.1016/j.bbrc.2005.10.212
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The mouse beta PIX-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 all overall conformation similar to the general SH3 structure. The X-ray structure shows Mouse beta PIX-SH3 domain binding the way in which the PPIX characteristic amino acids do so for ail unconventional ligand binding surface. This arrangement provides a rationale For the unusual ligand recognition motif exhibited by mouse beta PIX-SH3 domain. Comparison with mother SH3/peptide complex shows that the recognition mode of the mouse beta PIX-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 beta PIX-SH3 domain resulting in its multiple biological functions. (c) 2005 Elsevier Inc. All rights reserved.
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页码：407 / 414
页数：8
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