Source:http://linkedlifedata.com/resource/pubmed/id/10852922
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
45
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| pubmed:dateCreated |
2000-11-27
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| pubmed:abstractText |
Although crystallographic information is available on several nucleotide-induced states in myosin, little is known about the corresponding structural changes in kinesin, since a crystallographic model is only available for the kinesin:ADP complex. This makes it difficult to characterize at a molecular level the structural changes that occur in this motor through the course of its ATPase cycle. In this study, we report on the production of a series of single tryptophan mutants of a monomeric human kinesin motor domain, which demonstrate nucleotide-dependent changes in microtubule affinity that are similar to wild type. We have used these mutations to measure intramolecular distances in both strong and weak binding states, using fluorescence resonance energy transfer. This work provides direct evidence that movement of the switch II loop and helix are essential to mediate communication between the catalytic and microtubule binding sites, evidence that is supported as well by molecular modeling. Kinetic studies of fluorescent nucleotide binding to these mutants are consistent with these distance changes, and demonstrate as well that binding of ADP produces two structural transitions, neither of which are identical to that produced by the binding of ATP. This study provides a basis for understanding current structural models of the kinesin mechanochemical cycle.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Kinesin,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Tryptophan
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
10
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| pubmed:volume |
275
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
35413-23
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10852922-Adenosine Diphosphate,
pubmed-meshheading:10852922-Adenosine Triphosphatases,
pubmed-meshheading:10852922-Binding Sites,
pubmed-meshheading:10852922-Catalytic Domain,
pubmed-meshheading:10852922-Computer Simulation,
pubmed-meshheading:10852922-Crystallography, X-Ray,
pubmed-meshheading:10852922-Humans,
pubmed-meshheading:10852922-Kinesin,
pubmed-meshheading:10852922-Kinetics,
pubmed-meshheading:10852922-Microtubules,
pubmed-meshheading:10852922-Models, Biological,
pubmed-meshheading:10852922-Models, Molecular,
pubmed-meshheading:10852922-Mutagenesis, Site-Directed,
pubmed-meshheading:10852922-Nucleotides,
pubmed-meshheading:10852922-Protein Conformation,
pubmed-meshheading:10852922-Protein Structure, Tertiary,
pubmed-meshheading:10852922-Spectrometry, Fluorescence,
pubmed-meshheading:10852922-Time Factors,
pubmed-meshheading:10852922-Tryptophan
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| pubmed:year |
2000
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| pubmed:articleTitle |
Kinesin has three nucleotide-dependent conformations. Implications for strain-dependent release.
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| pubmed:affiliation |
Departments of Biochemistry and Molecular Genetics and Neurology and the Graduate Program in Cell and Molecular Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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