1h1w

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spinqualitylabelsall models 1h1w, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HIGH RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN PDK1 CATALYTIC DOMAIN

Overview

3-phosphoinositide dependent protein kinase-1 (PDK1) plays a key role in, regulating signalling pathways by activating AGC kinases such as PKB/Akt, and S6K. Here we describe the 2.0 A crystal structure of the PDK1 kinase, domain in complex with ATP. The structure defines the hydrophobic pocket, termed the "PIF-pocket", which plays a key role in mediating the, interaction and phosphorylation of certain substrates such as S6K1., Phosphorylation of S6K1 at its C-terminal PIF-pocket-interacting motif, promotes the binding of S6K1 with PDK1. In the PDK1 structure, this pocket, is occupied by a crystallographic contact with another molecule of PDK1., Interestingly, close to the PIF-pocket in PDK1, there is an ordered, sulfate ion, interacting tightly with four surrounding side chains. The, ... [(full description)]

About this Structure

1H1W is a [Single protein] structure of sequence from [Homo sapiens] with SO4, ATP and GOL as [ligands]. Active as [[1]], with EC number [2.7.1.37]. Full crystallographic information is available from [OCA].

Reference

High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site., Biondi RM, Komander D, Thomas CC, Lizcano JM, Deak M, Alessi DR, van Aalten DM, EMBO J. 2002 Aug 15;21(16):4219-28. PMID:12169624

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