1w1g
CRYSTAL STRUCTURE OF THE PDK1 PLECKSTRIN HOMOLOGY (PH) DOMAIN BOUND TO DIC4-PHOSPHATIDYLINOSITOL (3,4,5)-TRISPHOSPHATE
|
OverviewOverview
3-phosphoinositide-dependent protein kinase-1 (PDK1) phosphorylates and, activates many kinases belonging to the AGC subfamily. PDK1 possesses a, C-terminal pleckstrin homology (PH) domain that interacts with, PtdIns(3,4,5)P3/PtdIns(3,4)P2 and with lower affinity to PtdIns(4,5)P2. We, describe the crystal structure of the PDK1 PH domain, in the absence and, presence of PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4. The structures reveal a, 'budded' PH domain fold, possessing an N-terminal extension forming an, integral part of the overall fold, and display an unusually spacious, ligand-binding site. Mutagenesis and lipid-binding studies were used to, define the contribution of residues involved in phosphoinositide binding., Using a novel quantitative binding assay, we found that Ins(1,3,4,5,6)P5, ... [(full description)]
About this StructureAbout this Structure
1W1G is a [Single protein] structure of sequence from [Homo sapiens] with 4PT as [ligand]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates., Komander D, Fairservice A, Deak M, Kular GS, Prescott AR, Peter Downes C, Safrany ST, Alessi DR, van Aalten DM, EMBO J. 2004 Oct 13;23(20):3918-28. Epub 2004 Sep 30. PMID:15457207
Page seeded by OCA on Mon Oct 29 19:56:29 2007