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Science 13 July 2007:
Vol. 317. no. 5835, p. 165
DOI: 10.1126/science.317.5835.165h
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This Week in Science

Figure 1 Many human cancers involve gain-of-function mutations in the phosphoinositide 3-kinase PI3Kalpha. The kinase is a heterodimer of a catalytic subunit (p110alpha) and a regulatory subunit (p85alpha), with both subunits comprising multiple domains. Miled et al. (p. 239; see the Perspective by Lee et al.) have determined the crystal structure of the adaptor-binding domain of p110alpha bound to the inter-SH2 domain of p85alpha at 2.4 angstrom resolution, and have performed functional studies to investigate the effect of oncogenic mutations in the helical domain of p110alpha on its interaction with the N-terminal SH2 domain of p85alpha. The studies suggest how these two classes of mutations cause the up-regulation of PI3Kalpha that can lead to cancer.

CREDIT: MILED ET AL.




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Science. ISSN 0036-8075 (print), 1095-9203 (online)