Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains? - PubMed (original) (raw)

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

C P Ponting. Protein Sci. 1996 Nov.

Abstract

Two SH3 domain-containing cytosolic components of the NADPH oxidase, p47phox and p40phox, 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, p67phox, is shown to contain four tetratricopeptide repeats (TPRs) within its N-terminal RaclGTP-binding region, and a 28 residue motif in p40phox is demonstrated to be present in protein kinase C isoforms iota/lambda and zeta, and in three ZZ domain-containing proteins.

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References

    1. Curr Biol. 1995 Dec 1;5(12):1404-15 - PubMed
    1. Mol Cell Biol. 1996 Aug;16(8):4095-106 - PubMed
    1. Trends Biochem Sci. 1996 Jan;21(1):11-13 - PubMed
    1. Proc Natl Acad Sci U S A. 1989 May;86(9):3099-103 - PubMed
    1. J Clin Invest. 1989 Jun;83(6):1785-93 - PubMed

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