2biy | pdb_00002biy

STRUCTURE OF PDK1-S241A MUTANT KINASE DOMAIN

spinqualitylabelsall models 2biy, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2biy is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ATP, GOL, SO4 Related: 1h1w, 1oky, 1okz, 1uu3, 1uu7, 1uu8, 1uu9, 1uvr, 1w1d, 1w1g, 1w1h Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3-phosphoinositide-dependent protein kinase 1

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