1mkj

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{{STRUCTURE_1mkj| PDB=1mkj | SCENE= }}
{{STRUCTURE_1mkj| PDB=1mkj | SCENE= }}
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'''Human Kinesin Motor Domain With Docked Neck Linker'''
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===Human Kinesin Motor Domain With Docked Neck Linker===
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==Overview==
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Crystal structures of the molecular motor kinesin show conformational variability in a structural element called the neck linker. Conformational change in the neck linker, initiated by ATP exchange, is thought to drive the movement of kinesin along the microtubule track. We use site-specific EPR measurements to show that when microtubules are absent, the neck linker exists in equilibrium between two structural states (disordered and 'docked'). The active site nucleotide does not control the position taken by the neck linker. However, we find that sulfate can specifically bind near the nucleotide site and stabilize the docked neck linker conformation, which we confirmed by solving a new crystal structure. Comparing the crystal structures of our construct with the docked or undocked neck linker reveals how microtubule binding may activate the nucleotide-sensing mechanism of kinesin, allowing neck linker transitions to power motility.
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(as it appears on PubMed at http://www.pubmed.gov), where 12368902 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12368902}}
==About this Structure==
==About this Structure==
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[[Category: Relay helix]]
[[Category: Relay helix]]
[[Category: Switch ii]]
[[Category: Switch ii]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:11:34 2008''

Revision as of 21:11, 2 July 2008

Image:1mkj.png

Template:STRUCTURE 1mkj

Human Kinesin Motor Domain With Docked Neck Linker

Template:ABSTRACT PUBMED 12368902

About this Structure

1MKJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy., Sindelar CV, Budny MJ, Rice S, Naber N, Fletterick R, Cooke R, Nat Struct Biol. 2002 Nov;9(11):844-8. PMID:12368902

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