1h10
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(New page: 200px<br /> <applet load="1h10" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h10, resolution 1.40Å" /> '''HIGH RESOLUTION STR...)
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Revision as of 15:17, 29 October 2007
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HIGH RESOLUTION STRUCTURE OF THE PLECKSTRIN HOMOLOGY DOMAIN OF PROTEIN KINASE B/AKT BOUND TO INS(1,3,4,5)-TETRAKISPHOPHATE
Overview
The products of PI 3-kinase activation, PtdIns(3,4,5)P3 and its immediate, breakdown product PtdIns(3,4)P2, trigger physiological processes, by, interacting with proteins possessing pleckstrin homology (PH) domains. One, of the best characterized PtdIns(3,4,5)P3/PtdIns(3,4)P2 effector proteins, is protein kinase B (PKB), also known as Akt. PKB possesses a PH domain, located at its N terminus, and this domain binds specifically to, PtdIns(3,4,5)P3 and PtdIns(3,4)P2 with similar affinity. Following, activation of PI 3-kinase, PKB is recruited to the plasma membrane by, virtue of its interaction with PtdIns(3,4,5)P3/PtdIns(3,4)P2. PKB is then, activated by the 3-phosphoinositide-dependent pro-tein kinase-1 (PDK1), which like PKB, possesses a PtdIns(3,4,5)P3/PtdIns(3,4)P2 binding PH, domain. ... [(full description)]
About this Structure
1H10 is a [Single protein] structure of sequence from [Homo sapiens] with ACE and 4IP as [ligands]. Full crystallographic information is available from [OCA].
Reference
High-resolution structure of the pleckstrin homology domain of protein kinase b/akt bound to phosphatidylinositol (3,4,5)-trisphosphate., Thomas CC, Deak M, Alessi DR, van Aalten DM, Curr Biol. 2002 Jul 23;12(14):1256-62. PMID:12176338
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