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• W2791036101 abstract "Here, we study microscopic mechanism of complex formation between Ca2+-bound calmodulin (holoCaM) and Orai1 that regulates Ca2+-dependent inactivation process in eukaryotic cells. We compute conformational thermodynamic changes in holoCaM with respect to complex of Orai1 bound to C-terminal domain of holoCaM using histograms of dihedral angles of the proteins over trajectories from molecular dynamics simulations. Our analysis shows that the N-terminal domain residues L4, T5, Q41, N42, T44 and E67 of holoCaM get destabilized and disordered due to Orai1 binding to C-terminal domain of calmodulin affect the N-terminal domain residues. Among these residues, polar T44, having maximum destabilization and disorder via backbone fluctuations, shows the largest change in solvent exposure. This suggests that N-terminal domain is allosterically regulated via T44 by the binding of Orai1 to the C-terminal domain." @default.
• W2791036101 created "2018-03-29" @default.
• W2791036101 creator A5008283401 @default.
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• W2791036101 date "2018-02-15" @default.
• W2791036101 modified "2023-10-03" @default.
• W2791036101 title "Allostery in Orai1 binding to calmodulin revealed from conformational thermodynamics" @default.
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• W2791036101 doi "https://doi.org/10.1080/07391102.2018.1430617" @default.
• W2791036101 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29347889" @default.
• W2791036101 hasPublicationYear "2018" @default.
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