A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses

Cell. 1989 Mar 10;56(5):879-89. doi: 10.1016/0092-8674(89)90692-2.


The structure and function of kinesin heavy chain from D. melanogaster have been studied using DNA sequence analysis and analysis of the properties of truncated kinesin heavy chain synthesized in vitro. Analysis of the sequence suggests the existence of a 50 kd globular amino-terminal domain that contains an ATP binding consensus sequence, followed by another 50-60 kd domain that has sequence characteristics consistent with the ability to fold into an alpha helical coiled coil. The properties of amino- and carboxy-terminally truncated kinesin heavy chains synthesized in vitro reveal that a 60 kd amino-terminal fragment has the nucleotide-dependent microtubule binding activities of the intact kinesin heavy chain, and hence is likely to be a "motor" domain. Finally, the sequence data indicate the presence of a small carboxy-terminal domain. Because it is located at the end of the molecule away from the putative "motor" domain, we propose that this domain is responsible for interactions with other proteins, vesicles, or organelles. These data suggest that kinesin has an organization very similar to that of myosin even though there are no obvious sequence similarities between the two molecules.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics*
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • DNA Mutational Analysis
  • Drosophila melanogaster
  • Hydrogen Bonding
  • Kinesin
  • Microtubules / metabolism*
  • Microtubules / ultrastructure
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Nerve Tissue Proteins / ultrastructure*
  • Protein Biosynthesis
  • Structure-Activity Relationship


  • Nerve Tissue Proteins
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Kinesin

Associated data

  • GENBANK/M24441