1uu3: Difference between revisions

Revision as of 09:16, 29 July 2008

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File:1uu3.png

Template:STRUCTURE 1uu3

STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH LY333531STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH LY333531

Template:ABSTRACT PUBMED 14962382

About this StructureAbout this Structure

1UU3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Interactions of LY333531 and other bisindolyl maleimide inhibitors with PDK1., Komander D, Kular GS, Schuttelkopf AW, Deak M, Prakash KR, Bain J, Elliott M, Garrido-Franco M, Kozikowski AP, Alessi DR, van Aalten DM, Structure. 2004 Feb;12(2):215-26. PMID:14962382

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH LY333531'''
+===STRUCTURE OF HUMAN PDK1 KINASE DOMAIN IN COMPLEX WITH LY333531===
-==Overview==
+<!--
-LY333531, BIM-1, BIM-2, BIM-3, and BIM-8 are bisindolyl maleimide-based, nanomolar protein kinase C inhibitors. LY333531, a PKCbeta-specific inhibitor, is in clinical trials against diabetes and cardiac ventricular hypertrophy complications. Specificity analysis with a panel of 29 protein kinases reveals that these bisindolyl maleimide inhibitors also inhibit PDK1, a key kinase from the insulin signaling pathway, albeit in the lower microM range. To understand the molecular basis of inhibition, the PDK1 kinase domain was cocrystallized with these bisindolyl maleimide inhibitors. The inhibitor complexes represent the first structural description of this class of compounds, revealing their unusual nonplanar conformation within the ATP binding site and also explaining the higher inhibitory potential of LY33331 compared to the BIM compounds toward PDK1. A combination of site-directed mutagenesis and essential dynamics analysis gives further insight into PDK1 and also PKC inhibition by these compounds, and may aid inhibitor design.
+The line below this paragraph, {{ABSTRACT_PUBMED_14962382}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14962382 is the PubMed ID number.
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
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