Abstract
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 language | English |
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Pages (from-to) | 526-530 |
Number of pages | 5 |
Journal | Nature Structural Biology |
Volume | 8 |
Issue number | 6 |
DOIs | |
Publication status | Published - 2001 |
All Science Journal Classification (ASJC) codes
- Structural Biology
- Biochemistry
- Genetics