2biy

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[[Image:2biy.gif|left|200px]]<br /><applet load="2biy" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2biy.gif|left|200px]]
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caption="2biy, resolution 1.95&Aring;" />
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'''STRUCTURE OF PDK1-S241A MUTANT KINASE DOMAIN'''<br />
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{{Structure
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|PDB= 2biy |SIZE=350|CAPTION= <scene name='initialview01'>2biy</scene>, resolution 1.95&Aring;
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|SITE= <scene name='pdbsite=BC6:Atp+Binding+Site+For+Chain+A'>BC6</scene>
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|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>
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|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]
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|GENE=
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}}
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'''STRUCTURE OF PDK1-S241A MUTANT KINASE DOMAIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BIY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Known structural/functional Site: <scene name='pdbsite=BC6:Atp+Binding+Site+For+Chain+A'>BC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIY OCA].
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2BIY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BIY OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15741170 15741170]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15741170 15741170]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:38:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:02:34 2008''

Revision as of 14:02, 20 March 2008

Image:2biy.gif


PDB ID 2biy

Drag the structure with the mouse to rotate
, 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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