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1nvs

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bower, M.J.]]
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[[Category: Bower, M J.]]
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[[Category: Concha, N.O.]]
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[[Category: Concha, N O.]]
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[[Category: Davis, S.T.]]
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[[Category: Davis, S T.]]
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[[Category: Green, S.M.]]
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[[Category: Green, S M.]]
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[[Category: Johanson, K.O.]]
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[[Category: Johanson, K O.]]
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[[Category: McDevitt, P.J.]]
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[[Category: McDevitt, P J.]]
[[Category: Zhao, B.]]
[[Category: Zhao, B.]]
[[Category: Zhao, H.]]
[[Category: Zhao, H.]]
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[[Category: Zhou, B.B.]]
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[[Category: Zhou, B B.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: UCM]]
[[Category: UCM]]
[[Category: chk1-sb218078 complex]]
[[Category: chk1-sb218078 complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:31:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:41 2008''

Revision as of 12:10, 21 February 2008


1nvs, resolution 1.8Å

Drag the structure with the mouse to rotate

The Complex Structure Of Checkpoint Kinase Chk1/SB218078

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

1NVS is a Single protein structure of sequence from Homo sapiens with and as ligands. 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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