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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate.

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 A 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 PtdIns(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 PtdIns(3)P binding to the p40(phox) PX domain.[1]

References

  1. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Bravo, J., Karathanassis, D., Pacold, C.M., Pacold, M.E., Ellson, C.D., Anderson, K.E., Butler, P.J., Lavenir, I., Perisic, O., Hawkins, P.T., Stephens, L., Williams, R.L. Mol. Cell (2001) [Pubmed]
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