1ian: Difference between revisions
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[[Image:1ian.gif|left|200px]] | [[Image:1ian.gif|left|200px]] | ||
'''HUMAN P38 MAP KINASE INHIBITOR COMPLEX''' | {{Structure | ||
|PDB= 1ian |SIZE=350|CAPTION= <scene name='initialview01'>1ian</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=D13:4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE'>D13</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HUMAN P38 MAP KINASE INHIBITOR COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IAN is a [ | 1IAN 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=1IAN OCA]. | ||
==Reference== | ==Reference== | ||
A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket., Tong L, Pav S, White DM, Rogers S, Crane KM, Cywin CL, Brown ML, Pargellis CA, Nat Struct Biol. 1997 Apr;4(4):311-6. PMID:[http:// | A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket., Tong L, Pav S, White DM, Rogers S, Crane KM, Cywin CL, Brown ML, Pargellis CA, Nat Struct Biol. 1997 Apr;4(4):311-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9095200 9095200] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: serine/threonine-protein kinase]] | [[Category: serine/threonine-protein kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:47:46 2008'' |
Revision as of 12:47, 20 March 2008
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, resolution 2.0Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
HUMAN P38 MAP KINASE INHIBITOR COMPLEX
OverviewOverview
The crystal structure of human p38 mitogen-activated protein (MAP) kinase in complex with a potent and highly specific pyridinyl-imidazole inhibitor has been determined at 2.0 A resolution. The structure of the kinase, which is in its unphosphorylated state, is similar to that of the closely-related ERK2. The inhibitor molecule is bound in the ATP pocket. A hydrogen bond is made between the pyridyl nitrogen of the inhibitor and the main chain amido nitrogen of residue 109, analogous to the interaction from the N1 atom of ATP. The crystal structure provides possible explanations for the specificity of this class of inhibitors. Other protein kinase inhibitors may achieve their specificity through a similar mechanism. The structure also reveals a possible second binding site for this inhibitor, with currently unknown function.
About this StructureAbout this Structure
1IAN is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket., Tong L, Pav S, White DM, Rogers S, Crane KM, Cywin CL, Brown ML, Pargellis CA, Nat Struct Biol. 1997 Apr;4(4):311-6. PMID:9095200
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