2biy
From Proteopedia
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|PDB= 2biy |SIZE=350|CAPTION= <scene name='initialview01'>2biy</scene>, resolution 1.95Å | |PDB= 2biy |SIZE=350|CAPTION= <scene name='initialview01'>2biy</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=BC6:Atp+Binding+Site+For+Chain+A'>BC6</scene> | |SITE= <scene name='pdbsite=BC6:Atp+Binding+Site+For+Chain+A'>BC6</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] | |ACTIVITY= [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.11.1 Transferred entry: 2.7.11.1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.37 2.7.1.37] | ||
|GENE= | |GENE= | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:45:26 2008'' |
Revision as of 12:45, 23 March 2008
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| , 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
Page seeded by OCA on Sun Mar 23 14:45:26 2008
Categories: Homo sapiens | Single protein | Transferred entry: 2 7.11 1 | 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
