Distance Differences in the Helix II/III Interface of the Myosin Essential Light Chain Domains

Comparison of the Differences between the Two domains of Apo Calmodulin in the I/II Interface with the Difference between the Two Domains of Myosin Essential Light Chain in the Same Interface

A comparison of the II/III interhelical interface of the N- and C-terminal domains of apo calmodulin and of the myosin essential light chain: Interhelical distance difference matrix (DDM) entries are mapped onto ribbon representations of myosin ELC-N and of apo CaM-N. Residues that are moderately closer together in the N terminal domain (DD between -2 and -5 angstroms) are connected by light blue lines. Residues that are much closer together in N terminal domain (DDs than -5 angstroms) are connected by dark blue lines. Residues that are moderately closer together in C terminal domain (DD between 2 and 5 angstroms) are connected by light pink lines. Residues that are much closer together in the C terminal domain (DDs greaterthan 5 angstroms) are shown in magenta. The helices were rendered as ribbons using InsightII (MSI, San Diego, CA), and the DDs and contacts were rendered as distance restraints using the NMR_Refine module of InsightII. Coordinates are from PDB files 1CFC (apo calmodulin) and 1WDC (essential light chain).

There is also a graphic showing the distance differences and interhelical contacts in all of the interhelical interfaces of the two domains of the essential light chain, and a graphic showing the full distance difference matrix and interhelical contacts analysis comparing this nterface in the two domains of apo calmodulin.

Details about file locations and color scheme. Internal access only