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1q0b

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(New page: 200px<br /> <applet load="1q0b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q0b, resolution 1.9&Aring;" /> '''Crystal structure of...)
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Revision as of 16:42, 12 November 2007

Image:1q0b.gif

1q0b, resolution 1.9Å

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Crystal structure of the motor protein KSP in complex with ADP and monastrol

Overview

We report here the first inhibitor-bound structure of a mitotic motor, protein. The 1.9 A resolution structure of the motor domain of KSP, bound, with the small molecule monastrol and Mg2+ x ADP, reveals that monastrol, confers inhibition by "induced-fitting" onto the protein some 12 A away, from the catalytic center of the enzyme, resulting in the creation of a, previously non-existing binding pocket. The structure provides new, insights into the biochemical and mechanical mechanisms of the mitotic, motor domain. Inhibition of KSP provides a novel mechanism to arrest, mitotic spindle formation, a target of several approved and investigative, anti-cancer agents. The structural information gleaned from this novel, pocket offers a new angle for the design of anti-mitotic agents.

About this Structure

1Q0B is a Single protein structure of sequence from Homo sapiens with MG, ADP and NAT as ligands. Full crystallographic information is available from OCA.

Reference

Inhibition of a mitotic motor protein: where, how, and conformational consequences., Yan Y, Sardana V, Xu B, Homnick C, Halczenko W, Buser CA, Schaber M, Hartman GD, Huber HE, Kuo LC, J Mol Biol. 2004 Jan 9;335(2):547-54. PMID:14672662

Page seeded by OCA on Mon Nov 12 18:49:13 2007

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