451. Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain.
- Author
-
Stevenson MA and Calderwood SK
- Subjects
- Amino Acid Sequence, Animals, Binding, Competitive, Biological Assay, Calcium metabolism, Enzyme Activation drug effects, In Vitro Techniques, Mice, Molecular Sequence Data, Multigene Family, Oligopeptides chemical synthesis, Oligopeptides metabolism, Phosphoric Diester Hydrolases metabolism, Calmodulin metabolism, Heat-Shock Proteins metabolism
- Abstract
The 70-kilodalton heat shock protein (hsp70) family members appear to be essential components in a number cellular protein-protein interactions. We report here on the characterization of a new functional region in hsp70, a calmodulin-binding site. We have identified a 21-amino-acid sequence within the hsp70 protein that contains a calmodulin-binding domain. The peptide formed a potential amphipathic alpha helix and bound calmodulin with high affinity. Comparison of amino acid homology of this calmodulin-binding sequence with analogous hsp70 sequences from other species showed a high degree of conservation.
- Published
- 1990
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