Abstract
Myosin light chain kinase contains a regulatory segment consisting of an autoinhibitory region and a calmodulin-binding sequence that folds back on its catalytic core to inhibit kinase activity. It has been proposed that α-helix formation may be involved in displacement of the regulatory segment and activation of the kinase by Ca2+/calmodulin. Proline mutations were introduced at putative non-interacting residues in the regulatory segment to disrupt helix formation. Substitution of proline residues immediately N-terminal of the Trp in the calmodulin-binding sequence had most significant effects on Ca2+/calmodulin binding and activation. Formation of an α-helix in this region upon Ca2+/calmodulin binding may be necessary for displacement of the regulatory segment allowing phosphorylation of myosin regulatory light chain. Copyright (C) 2000 Federation of European Biochemical Societies.
Original language | English (US) |
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Pages (from-to) | 148-152 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 472 |
Issue number | 1 |
DOIs | |
State | Published - Apr 21 2000 |
Keywords
- Activation
- Autoinhibition
- Calmodulin
- Helix
- Myosin light chain kinase
- Proline
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology