Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.

ABSTRACT: Calmodulin (CaM) mediates a wide range of biological responses to changes in intracellular Ca²⁺ concentrations through its calcium-dependent binding affinities to numerous target proteins. Binding of two Ca²⁺ ions to each of the two four-helix-bundle domains of CaM results in major conformational changes that create a potential binding site for the CaM binding domain of a target protein, which also undergoes major conformational changes to form the complex with CaM. Details of the molecular mechanism of complex formation are not well established, despite numerous structural, spectroscopic, thermodynamic, and kinetic studies. Here, we report a study of the process by which the 26-residue peptide M13, which represents the CaM binding domain of skeletal muscle myosin lig

SUBMITTER: Jeon J 

PROVIDER: S-EPMC8462368 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature