2biy | pdb_00002biy
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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., ... [(full description)]
About this Structure
2BIY 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
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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Proteopedia Page Contributors and Editors (what is this?)
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- Homo sapiens
- Single protein
- Aalten, D.M.F.Van.
- Alessi, D.R.
- Deak, M.
- Komander, D.
- Kular, G.S.
- ATP
- GOL
- SO4
- Ac-helix
- Agc kinase
- Atp-binding
- Phosphoinositide dependent protein kinase
- Phosphorylation
- Pi3-kinase signalling
- Pif-pocket
- Pka
- Pkb
- Serine-threonine-protein kinase
- T-loop mutant
- Transferase
