| Protein |
Species |
Information |
Comment |
Submitted By |
Validated By |
|---|---|---|---|---|---|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
Information about the activation of smooth muscle myosin light chain kinase by this protein:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
biochemical evidence of interaction with smooth muscle myosin light chain kinase:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
Information about the activation of skeletal muscle myosin light chain kinase by this protein:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
Information about the activation of neuronal nitric oxide synthase by this protein:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
biochemical evidence of interaction with neuronal nitric oxide synthase:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 the main isoform, and the only isoform found in most species |
Bos taurus (cow or bovine) |
Report of an engineered mutant with following mutations:
|
Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |
|
| calmodulin isoform 1 mutant:
|
Bos taurus (cow or bovine) |
Deletion of residues 2-8 from the N-terminal leader sequence abolishes the ability of calmodulin to activate skeletal myosin light chain kinase and reduces the ability of calmodulin to activate smooth muscle myosin light chain kinase to about 50% of maximum. This deletion does not affect the ability of calmodulin to activate cerebellar nitric oxide synthase. Overlapping tripeptide deletions indicate that residues 6-8 (E6,E7, and Q8) are the important residues for activation of skMLCK | Melanie R. Nelson The Scripps Research Institute, Department of Molecular Biology mnelson@scripps.edu |
Melanie R. Nelson mnelson@scripps.edu |