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PMID: 11316608 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review

The dynein heavy chain: structure, mechanics and evolution.

Trends in cell biology ·Vol. 11 ·No. 5 ·2001-05-00 ·Pages 196-202

Asai DJ, Koonce MP

Abstract

The translocation of dynein along microtubules is the basis for a variety of essential cellular movements. Despite a general domain organization that is found in all the cytoskeletal motors, there are structural features of dynein that set it apart from the other motors. These include a track-binding site that is located at the tip of a long projection, and six nucleotide-binding modules that together form the globular head of dynein. These unique features suggest that dynein produces movement by a mechanism that is different from that used by the other motors.

MeSH Terms
Amino Acid Sequence Animals Dyneins/chemistry,metabolism,ultrastructure Evolution, Molecular Humans Microtubules/metabolism Models, Molecular Molecular Motor Proteins/physiology Molecular Sequence Data Protein Binding Protein Conformation
Chemicals
Molecular Motor Proteins Dyneins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Asai D J
Dept of Biological Sciences, Purdue University, Lilly Hall, West Lafayette, IN 47907-1392, USA. dasai@bilbo.bio.purdue.edu
Koonce M P
Article Info
Journal
Trends in cell biology
Abbr.
Trends Cell Biol
ISSN
0962-8924
Published
2001-05-00
Pages
196-202
Language
English
Region
England
NLM ID
9200566
Subset
IM
Grants
NIGMS NIH HHS · GM51532 · United States
Databases
GENBANK
AL031546, P90736, U53876
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