1nvr: Difference between revisions
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|PDB= 1nvr |SIZE=350|CAPTION= <scene name='initialview01'>1nvr</scene>, resolution 1.8Å | |PDB= 1nvr |SIZE=350|CAPTION= <scene name='initialview01'>1nvr</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=STU:STAUROSPORINE'>STU</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1nvq|1nvq]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvr OCA], [http://www.ebi.ac.uk/pdbsum/1nvr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nvr RCSB]</span> | |||
}} | }} | ||
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[[Category: Zhao, H.]] | [[Category: Zhao, H.]] | ||
[[Category: Zhou, B B.]] | [[Category: Zhou, B B.]] | ||
[[Category: chk1-staurosporine complex]] | [[Category: chk1-staurosporine complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:36:12 2008'' | ||
Revision as of 22:36, 30 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1nvq
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Complex Structure Of Checkpoint Kinase Chk1/Staurosporine
OverviewOverview
Chk1 is a serine-threonine kinase that plays an important role in the DNA damage response, including G(2)/M cell cycle control. UCN-01 (7-hydroxystaurosporine), currently in clinical trials, has recently been shown to be a potent Chk1 inhibitor that abrogates the G(2)/M checkpoint induced by DNA-damaging agents. To understand the structural basis of Chk1 inhibition by UCN-01, we determined the crystal structure of the Chk1 kinase domain in complex with UCN-01. Chk1 structures with staurosporine and its analog SB-218078 were also determined. All three compounds bind in the ATP-binding pocket of Chk1, producing only slight changes in the protein conformation. Selectivity of UCN-01 toward Chk1 over cyclin-dependent kinases can be explained by the presence of a hydroxyl group in the lactam moiety interacting with the ATP-binding pocket. Hydrophobic interactions and hydrogen-bonding interactions were observed in the structures between UCN-01 and the Chk1 kinase domain. The high structural complementarity of these interactions is consistent with the potency and selectivity of UCN-01.
About this StructureAbout this Structure
1NVR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for Chk1 inhibition by UCN-01., Zhao B, Bower MJ, McDevitt PJ, Zhao H, Davis ST, Johanson KO, Green SM, Concha NO, Zhou BB, J Biol Chem. 2002 Nov 29;277(48):46609-15. Epub 2002 Sep 19. PMID:12244092
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