Document Detail

Limping of homodimeric kinesin motors.
MedLine Citation:
PMID:  17188298     Owner:  NLM     Status:  MEDLINE    
Conventional kinesin, a homodimeric motor protein that transports cargo in various cells, walks limpingly along microtubule. Here, based on our previously proposed partially coordinated hand-over-hand model, we present a new mechanism for the limping behaviors of both wild-type and mutant kinesin homodimers. The limping is caused by different vertical forces acting on the heads in two successive steps during the processive movement of the dimer. From the model, various theoretical results, such as the dependences of the mean dwell time and dwell time ratio on the coiled-coil length and on the external load as well as the effect of vertical force on velocity, are in good agreement with previous experimental results. We predict that a high degree of limping will correlate strongly with a high sensitivity of ATP turnover rate to upwards force.
Ping Xie; Shuo-Xing Dou; Peng-Ye Wang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-10-28
Journal Detail:
Title:  Journal of molecular biology     Volume:  366     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2007 Feb 
Date Detail:
Created Date:  2007-02-05     Completed Date:  2007-03-29     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  976-85     Citation Subset:  IM    
Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing, China.
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MeSH Terms
Drosophila melanogaster
Kinesin / chemistry*,  metabolism*
Microtubules / metabolism
Models, Molecular
Molecular Motor Proteins / chemistry*,  metabolism*
Protein Structure, Secondary
Protein Structure, Tertiary
Time Factors
Reg. No./Substance:
0/Molecular Motor Proteins; EC 3.6.1.-/Kinesin

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