2biy

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spinqualitylabelsall models PDB ID 2biy Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 1.95Å
Sites:
Ligands:	, and
Activity:	Transferred entry: 2.7.11.1, with EC number 2.7.1.37
Coordinates:	save as pdb, mmCIF, xml

STRUCTURE OF PDK1-S241A MUTANT KINASE DOMAIN

Overview

3-Phosphoinositide-dependent protein kinase-1 (PDK1) phosphorylates the T-loop of several AGC (cAMP-dependent, cGMP-dependent, protein kinase C) family protein kinases, resulting in their activation. Previous structural studies have revealed that the alpha C-helix, located in the small lobe of the kinase domain of PDK1, is a key regulatory element, as it links a substrate interacting site termed the hydrophobic motif (HM) pocket with the phosphorylated Ser-241 in the T-loop. In this study we have demonstrated by mutational analysis that interactions between the phosphorylated Ser-241 and the alpha C-helix are not required for PDK1 activity or substrate binding through the HM-pocket but are necessary for PDK1 to be activated or stabilized by a peptide that binds to this site. The structure of an inactive T-loop mutant of PDK1, in which Ser-241 is changed to Ala, was also determined. This structure, together with surface plasmon resonance binding studies, demonstrates that the PDK1(S241A)-inactive mutant possesses an intact HM-pocket as well as an ordered alpha C-helix. These findings reveal that the integrity of the alpha C-helix and HM-pocket in PDK1 is not regulated by T-loop phosphorylation.

About this Structure

2BIY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Role of T-loop phosphorylation in PDK1 activation, stability, and substrate binding., Komander D, Kular G, Deak M, Alessi DR, van Aalten DM, J Biol Chem. 2005 May 13;280(19):18797-802. Epub 2005 Mar 1. PMID:15741170

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