Abstract
Smooth muscle myosin light chain kinase (MLCK) plays important roles in contractile-motile processes of a variety of cells. Three DFRxxL motifs at the kinase N-terminus (residues 2-63) are critical for high-affinity binding to actin-containing filaments [Smith et al. (1999) J. Biol. Chem. 274, 29433- 29438]. A GST fusion protein containing residues 1-75 of MLCK (GST75-MLCK) bound maximally to both smooth muscle myofilaments and F-actin at 0.28 and 0.31 mol GST75-MLCK/mol actin with respective K(D) values of 0.1 μM and 0.8 μM. High-affinity binding of MLCK to actin-containing filaments may be due to each DFRxxL motif binding to one actin monomer in filaments. (C) 2000 Federation of European Biochemical Societies.
Original language | English (US) |
---|---|
Pages (from-to) | 298-300 |
Number of pages | 3 |
Journal | FEBS Letters |
Volume | 480 |
Issue number | 2-3 |
DOIs | |
State | Published - Sep 1 2000 |
Keywords
- Actin
- Calcium
- Calmodulin
- Myofilament
- Myosin light chain kinase
ASJC Scopus subject areas
- Biophysics
- Structural Biology
- Biochemistry
- Molecular Biology
- Genetics
- Cell Biology