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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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<applet load="1q0b" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1q0b, resolution 1.9&Aring;" />
'''Crystal structure of the motor protein KSP in complex with ADP and monastrol'''<br />
'''Crystal structure of the motor protein KSP in complex with ADP and monastrol'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1Q0B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG, ADP and NAT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q0B OCA].
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1Q0B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ADP:'>ADP</scene> and <scene name='pdbligand=NAT:'>NAT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q0B OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Buser, C.A.]]
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[[Category: Buser, C A.]]
[[Category: Halczenko, W.]]
[[Category: Halczenko, W.]]
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[[Category: Hartman, G.D.]]
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[[Category: Hartman, G D.]]
[[Category: Homnick, C.]]
[[Category: Homnick, C.]]
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[[Category: Huber, H.E.]]
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[[Category: Huber, H E.]]
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[[Category: Kuo, L.C.]]
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[[Category: Kuo, L C.]]
[[Category: Sardana, V.]]
[[Category: Sardana, V.]]
[[Category: Xu, B.]]
[[Category: Xu, B.]]
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[[Category: motor protein]]
[[Category: motor protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:49:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:29 2008''

Revision as of 12:34, 21 February 2008

Image:1q0b.gif

1q0b, resolution 1.9Å

Drag the structure with the mouse to rotate

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 , and 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 Thu Feb 21 14:34:29 2008

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