Energetic and structural insights behind calcium induced conformational transition in calmodulin.

ABSTRACT: Calmodulin (CaM) is a key signaling protein that triggers several cellular and physiological processes inside the cell. Upon binding with calcium ion, CaM undergoes large scale conformational transition from a closed state to an open state that facilitates its interaction with various target protein and regulates their activity. This work explores the origin of the energetic and structural variation of the wild type and mutated CaM and explores the molecular origin for the structural differences between them. We first calculated the sequential calcium binding energy to CaM using the PDLD/S-LRA/β approach. This study  shows a very good correlation with experimental calcium binding energies. Next we calculated the calcium binding energies to the wild type CaM and several mutated CaM systems

SUBMITTER: Halder R 

PROVIDER: S-EPMC10872638 | biostudies-literature | 2024 Mar

REPOSITORIES: biostudies-literature