Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3‐kinases: Binding partners of SH3 domains?
Open Access
- 1 November 1996
- journal article
- for the-record
- Published by Wiley in Protein Science
- Vol. 5 (11) , 2353-2357
- https://doi.org/10.1002/pro.5560051122
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 τ/λ and ζ, and in three ZZ domain‐containing proteins.Keywords
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