期刊
MOLECULAR CELL
卷 8, 期 4, 页码 829-839出版社
CELL PRESS
DOI: 10.1016/S1097-2765(01)00372-0
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资金
- MRC [MC_U105184308] Funding Source: UKRI
- Medical Research Council [MC_U105184308] Funding Source: researchfish
More than 50 human proteins with a wide range of functions have a 120 residue phosphoinositide binding module known as the PX domain. The 1.7 Angstrom X-ray crystal structure of the PX domain from the p40(phox) subunit of NADPH oxidase bound to PtdIns(3)P shows that the PX domain embraces the 3-phosphate on one side of a water-filled, positively charged pocket and reveals how 3-phosphoinositide specificity is achieved. A chronic granulomatous disease (CGD)-associated mutation in the p47(phox) PX domain that abrogates Ptdlns(3)P binding maps to a conserved Arg that does not directly interact with the phosphoinositide but instead appears to stabilize a critical lipid binding loop. The SH3 domain present in the full-length protein does not affect soluble Ptdlns(3)P binding to the p40(phox) PX domain.
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