1nvq
From Proteopedia
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|PDB= 1nvq |SIZE=350|CAPTION= <scene name='initialview01'>1nvq</scene>, resolution 2.0Å | |PDB= 1nvq |SIZE=350|CAPTION= <scene name='initialview01'>1nvq</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=UCN:7-HYDROXYSTAUROSPORINE'>UCN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nvq OCA], [http://www.ebi.ac.uk/pdbsum/1nvq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nvq RCSB]</span> | ||
}} | }} | ||
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[[Category: Zhao, H.]] | [[Category: Zhao, H.]] | ||
[[Category: Zhou, B B.]] | [[Category: Zhou, B B.]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: UCN]] | ||
[[Category: chk1-ucn-01 complex]] | [[Category: chk1-ucn-01 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 22:36:13 2008'' |
Revision as of 19:36, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Complex Structure Of Checkpoint Kinase Chk1/UCN-01
Overview
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 Structure
1NVQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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