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

Citation
H. Hiroaki et al., Solution structure of the PX domain, a target of the SH3 domain, NAT ST BIOL, 8(6), 2001, pp. 526-530
Citations number
26
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
8
Issue
6
Year of publication
2001
Pages
526 - 530
Database
ISI
SICI code
1072-8368(200106)8:6<526:SSOTPD>2.0.ZU;2-X
Abstract
The phox homology (PX) domain is a novel protein module containing a conser ved proline-rich motif, We have shown that the PX domain isolated from the human p47(phox) protein, a soluble subunit of phagocyte NADPH oxidase, bind s specifically to the C-terminal SH3 domain derived from the same protein. The solution structure of p47 PX has an alpha + beta structure with a novel folding moth topology and reveals that the proline-rich motif is presented on the molecular surface for easy recognition by the SH3 domain. The proli ne-rich moth of p47 PX in the free state adopts a distorted left-handed pol yproline type II helix conformation.