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Trends Biochem Sci. 2002 Aug;27(8):426-32.

Structural insight into substrate specificity and regulatory mechanisms of phosphoinositide 3-kinases.

Author information

  • 1Bloomsbury Centre for Structural Biology and Department of Biochemistry and Molecular Biology, University College London, London, UK WC1E 6BT. snezana@biochem.ucl.ac.uk

Abstract

Phosphoinositide 3-kinases (PI3Ks) are implicated in a variety of fundamental cellular processes. These enzymes catalyse phosphorylation of the 3'-OH position of myo-inositol lipids that serve as secondary messengers. The catalytic subunit for one of the family members, PI3K gamma, has been structurally characterized, independently, in complexes with kinase inhibitors and with the p21(Ras) GTPase. These atomic structures provide a basis for the rationalization of some PI3K substrate specificities and regulatory mechanisms, establishing links to functional and cellular data. Ongoing comprehensive structural and functional studies are essential to realize the promise of PI3K isozyme-specific therapeutic agents.

PMID:
12151228
[PubMed - indexed for MEDLINE]
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