1ogu: Difference between revisions

Revision as of 16:39, 28 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:1ogu.png

Template:STRUCTURE 1ogu

STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITORSTRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR

Template:ABSTRACT PUBMED 12941338

About this StructureAbout this Structure

1OGU is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure-based design of 2-arylamino-4-cyclohexylmethyl-5-nitroso-6-aminopyrimidine inhibitors of cyclin-dependent kinases 1 and 2., Sayle KL, Bentley J, Boyle FT, Calvert AH, Cheng Y, Curtin NJ, Endicott JA, Golding BT, Hardcastle IR, Jewsbury P, Mesguiche V, Newell DR, Noble ME, Parsons RJ, Pratt DJ, Wang LZ, Griffin RJ, Bioorg Med Chem Lett. 2003 Sep 15;13(18):3079-82. PMID:12941338

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OCA

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-[[Image:1ogu.gif|left|200px]]
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-'''STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR'''
+===STRUCTURE OF HUMAN THR160-PHOSPHO CDK2/CYCLIN A COMPLEXED WITH A 2-ARYLAMINO-4-CYCLOHEXYLMETHYL-5-NITROSO-6-AMINOPYRIMIDINE INHIBITOR===
-==Overview==
+<!--
-A series of O(4)-cyclohexylmethyl-5-nitroso-6-aminopyrimidines bearing 2-arylamino substituents was synthesised and evaluated for CDK1 and CDK2 inhibitory activity. Consistent with analogous studies with O(6)-cyclohexylmethylpurines, 2-arylaminopyrimidines with a sulfonamide or carboxamide group at the 4'-position were potent inhibitors, with IC(50) values against CDK2 of 1.1+/-0.3 and 34+/-8 nM, respectively. The crystal structure of the 4'-carboxamide derivative, in complex with phospho-Thr160 CDK2/cyclin A, confirmed the expected binding mode of the inhibitor, and revealed an additional interaction between the carboxamide function and an aspartate residue.
+The line below this paragraph, {{ABSTRACT_PUBMED_12941338}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12941338 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12941338}}
 ==About this Structure==
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 [[Category: Serine/threonine-protein kinase]]
 [[Category: Transferase]]
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