Document Detail


The design plan of kinesin motors.
MedLine Citation:
PMID:  9442886     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The kinesin superfamily comprises a large and structurally diverse group of microtubule-based motor proteins that produce a variety of force-generating activities within cells. This review addresses how the structures of kinesin proteins provide clues as to their biological functions and motile properties. We discuss structural features common to all kinesin motors, as well as specialized features that enable subfamilies of related motors to carry out specialized activities. We also discuss how the kinesin motor domain uses chemical energy from ATP hydrolysis to move along microtubules.
Authors:
R D Vale; R J Fletterick
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.; Review    
Journal Detail:
Title:  Annual review of cell and developmental biology     Volume:  13     ISSN:  1081-0706     ISO Abbreviation:  Annu. Rev. Cell Dev. Biol.     Publication Date:  1997  
Date Detail:
Created Date:  1998-02-13     Completed Date:  1998-02-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9600627     Medline TA:  Annu Rev Cell Dev Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  745-77     Citation Subset:  IM    
Affiliation:
Howard Hughes Medical Institute, University of California, San Francisco 94143, USA. vale@phy.ucsf.edu
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphate / metabolism
Amino Acid Sequence
Animals
Energy Metabolism
Humans
Kinesin / chemistry*,  physiology
Macromolecular Substances
Molecular Sequence Data
Protein Conformation
Chemical
Reg. No./Substance:
0/Macromolecular Substances; 56-65-5/Adenosine Triphosphate; EC 3.6.1.-/Kinesin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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