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

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Pages (from-to)2353-7
Number of pages5
JournalProtein Science
Volume5
Issue number11
DOIs
Publication statusPublished - Nov 1996

Keywords

  • Amino Acid Sequence
  • Carrier Proteins
  • Humans
  • Molecular Sequence Data
  • NADPH Oxidase
  • Phosphatidylinositol 3-Kinases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Sequence Homology, Amino Acid
  • Vesicular Transport Proteins
  • src Homology Domains

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