Solution structure of the PX domain, a target of the SH3 domain

被引:145
作者
Hiroaki, H
Ago, T
Ito, T
Sumimoto, H
Kohda, D
机构
[1] Biomol Engn Res Inst, Dept Biol Struct, Osaka 5650874, Japan
[2] Kyushu Univ, Grad Sch Med Sci, Dept Mol & Struct Biol, Higashi Ku, Fukuoka 8120082, Japan
[3] Kanazawa Univ, Canc Res Inst, Kanazawa, Ishikawa 9200934, Japan
关键词
D O I
10.1038/88591
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 phox homology (PX) domain is a novel protein module containing a conserved proline-rich motif, We have shown that the PX domain isolated from the human p47(phox) protein, a soluble subunit of phagocyte NADPH oxidase, binds specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding moth topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich moth of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation.
引用
收藏
页码:526 / 530
页数:5
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