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

研究成果: ジャーナルへの寄稿記事

139 引用 (Scopus)

抄録

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.

元の言語英語
ページ(範囲)526-530
ページ数5
ジャーナルNature Structural Biology
8
発行部数6
DOI
出版物ステータス出版済み - 2001

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src Homology Domains
Proline
Proteins
NADPH Oxidase
Phagocytes
Conformations
Topology
4-ethoxymethylene-2-phenyl-2-oxazoline-5-one

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Structural Biology
  • Genetics

これを引用

Solution structure of the PX domain, a target of the SH3 domain. / Hiroaki, Hidekazu; Ago, Tetsuro; Ito, Takashi; Sumimoto, Hideki; Kohda, Daisuke.

:: Nature Structural Biology, 巻 8, 番号 6, 2001, p. 526-530.

研究成果: ジャーナルへの寄稿記事

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