1zyj: Difference between revisions

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[[Image:1zyj.~~gif~~|left|200px]]

[[Image:1zyj.png|left|200px]]

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~~'''~~Human P38 MAP Kinase in Complex with Inhibitor 1a~~'''~~

===Human P38 MAP Kinase in Complex with Inhibitor 1a===

~~==Overview==~~

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Two new classes of diphenylether inhibitors of p38alpha MAP kinase are described. Both chemical classes are based on a common diphenylether core that is identified by simulated fragment annealing as one of the most favored chemotypes within a prominent hydrophobic pocket of the p38alpha ATP-binding site. In the fully elaborated molecules, ~~the diphenylether moiety acts as an anchor occupying the deep pocket~~, ~~while polar extensions make specific interactions with either~~ the ~~adenine binding site or~~ the ~~phosphate binding site of ATP~~. ~~The synthesis~~, ~~crystallographic analysis, and biological activity of these p38alpha inhibitors are discussed~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16169718}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16169718 is the PubMed ID number.

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==About this Structure==

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[[Category: Springman, E B.]]

[[Category: Protein-inhibitor complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 18~~:14:27 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:11:29 2008''

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-[[Image:1zyj.gif|left|200px]]
+{{Seed}}
+[[Image:1zyj.png|left|200px]]
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 {{STRUCTURE_1zyj|  PDB=1zyj  |  SCENE=  }}
-'''Human P38 MAP Kinase in Complex with Inhibitor 1a'''
+===Human P38 MAP Kinase in Complex with Inhibitor 1a===
-==Overview==
+<!--
-Two new classes of diphenylether inhibitors of p38alpha MAP kinase are described. Both chemical classes are based on a common diphenylether core that is identified by simulated fragment annealing as one of the most favored chemotypes within a prominent hydrophobic pocket of the p38alpha ATP-binding site. In the fully elaborated molecules, the diphenylether moiety acts as an anchor occupying the deep pocket, while polar extensions make specific interactions with either the adenine binding site or the phosphate binding site of ATP. The synthesis, crystallographic analysis, and biological activity of these p38alpha inhibitors are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16169718}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16169718 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16169718}}
 ==About this Structure==
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 [[Category: Springman, E B.]]
 [[Category: Protein-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:14:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:11:29 2008''