Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: Binding partners of SH3 domains?

被引:253
作者
Ponting, CP
机构
[1] University of Oxford, Fibrinolysis Research Unit, Old Observatory, Oxford OX1 3RH, South Parks Road
关键词
homology; signal transduction; chronic granulomatous disease; tetratrico peptide repeats; phospholipase D;
D O I
10.1002/pro.5560051122
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
Two SH3 domain-containing cytosolic components of the NADPH oxidase, p47(phox) and p40(phox), are shown by analyses of their sequences to contain single copies of a novel class of domain, the PX (phox) domain. Homologous domains are demonstrated to be present in the Cpk class of phosphatidylinositol 3-kinase, S. cerevisiae Bem1p, and S. pombe Scd2, and a large family of human sorting nexin 1 (SNX1) homologues. The majority of these domains contains a polyproline motif, typical of SH3 domain-binding proteins. Two further findings are reported. A third NADPH oxidase subunit, p67(phox), is shown to contain four tetratricopeptide repeats (TPRs) within its N-terminal RaC1(GTP)-binding region, and a 28 residue motif in p40(phox) is demonstrated to be present in protein kinase C isoforms iota/lambda and zeta, and in three ZZ domain-containing proteins.
引用
收藏
页码:2353 / 2357
页数:5
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