Differences in the domain orientation of calmodulin in the complexes with the myosin light chain kinase peptide and the calmodulin kinase II peptide. The structure of the calmodulin complex with the eight residue CaMKII peptide is superimposed on the structure of the complex with the twelve residue MLCK peptide. The backbone atoms of the N-terminal domain of calmodulin in the two complexes were superimposed in panel a, and the backbone atoms of the C-terminal domain were superimposed in panel b. The two domains of calmodulin are seen to be closer together in the CaMKII complex than in the MLCK complex. Calmodulin is shown in light grey in the complex with the MLCK peptide and in medium grey in the complex with the CaMKII peptide. The MLCK peptide is dark grey, and the CaMKII peptide is black. The structures were superimposed and rendered in Insight using PDB coordinates 1CDL (MLCK complex) and 1CDM (CaMKII complex).
This figure appeared as figure 12 in the book chapter:
Nelson, M.R., Chazin W.J., "Calmodulin as a calcium sensor" in
Calmodulin and Signal Transduction (1998) L.J. Van Eldik and
D.M. Watterson, eds. Academic Press, San Diego, pp. 17-64.
Details about file locations and color scheme. Internal access only
 |
 |
 |
 |
 |
 |
 |
 |
 |
CaBP Data Library Home Page|
General Info|
Sequence Info|
Structural Info|
Analysis Tools
Top of Current Section|
Search the Data Library|
Site Map|
Feedback