Myosin essential light chain. Based on the analysis of the distance difference matrix and inter-residue contact analysis comparing the two domains of myosin essential light chain, a model of the conformational chainges induced by IQ-motif bidning is proposed. This model assumes that ELC-N is a good model for the closed conformation of ELC-C, and indeed that ELC-C actually adopts the closed conformation in the absence of IQ-motif containing ligand.
The IQ-motif (shown in yellow), binds to the C-terminal domain of ELC, making hydrogen bonds to the linker loopi (shown in pink) between helices II and III. This pulls the bottoms of helices II and III (shown in blue) together, which in turn pulls these two helices away from helices I and IV (shown in green). The PDB file used was 1WDC.
There is a graphic showing the distance differences and interhelical contacts in all interfaces of myosin ELC.
Details about file locations and color scheme. Internal access only
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