2oh0: Difference between revisions

Revision as of 05:28, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oh0.png

Template:STRUCTURE 2oh0

Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based InhibitorsCrystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based Inhibitors

Template:ABSTRACT PUBMED 17258463

About this StructureAbout this Structure

2OH0 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

Design and synthesis of pyridine-pyrazolopyridine-based inhibitors of protein kinase B/Akt., Zhu GD, Gong J, Gandhi VB, Woods K, Luo Y, Liu X, Guan R, Klinghofer V, Johnson EF, Stoll VS, Mamo M, Li Q, Rosenberg SH, Giranda VL, Bioorg Med Chem. 2007 Mar 15;15(6):2441-52. Epub 2007 Jan 17. PMID:17258463

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based Inhibitors'''
+===Crystal structure of Protein Kinase A in complex with Pyridine-Pyrazolopyridine Based Inhibitors===
-==Overview==
+<!--
-Thr-211 is one of three different amino acid residues in the kinase domain of protein kinase B/Akt as compared to protein kinase A (PKA), a closely related analog in the same AGC family. In an attempt to improve the potency and selectivity of our indazole-pyridine series of Akt inhibitors over PKA, efforts have focused on the incorporation of a chemical functionality to interact with the hydroxy group of Thr-211. Several substituents including an oxygen anion, amino, and nitro groups have been introduced at the C-6 position of the indazole scaffold, leading to a significant drop in Akt potency. Incorporation of a nitrogen atom into the phenyl ring at the same position (i.e., 9f) maintained the Akt activity and, in some cases, improved the selectivity over PKA. The structure-activity relationships of the new pyridine-pyrazolopyridine series of Akt inhibitors and their structural features when bound to PKA are also discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_17258463}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17258463 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17258463}}
 ==About this Structure==
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 [[Category: Akt]]
 [[Category: Protein kinase some]]
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