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

Hidekazu Hiroaki, Tetsuro Ago, Takashi Ito, Hideki Sumimoto, Daisuke Kohda

Research output: Contribution to journalArticlepeer-review

154 Citations (Scopus)


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 p47phox 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 cα + β structure with a novel folding motif topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proline-rich motif of p47 PX in the free state adopts a distorted left-handed polyproline type II helix conformation.

Original languageEnglish
Pages (from-to)526-530
Number of pages5
JournalNature Structural Biology
Issue number6
Publication statusPublished - 2001

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics


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