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• W2337942016 abstract "Calmodulin (CaM) is a ubiquitous Ca(2+) sensor and a crucial signalling hub in many pathways aberrantly activated in disease. However, the mechanistic basis of its ability to bind diverse signalling molecules including G-protein-coupled receptors, ion channels and kinases remains poorly understood. Here we harness the high resolution of molecular dynamics simulations and the analytical power of Markov state models to dissect the molecular underpinnings of CaM binding diversity. Our computational model indicates that in the absence of Ca(2+), sub-states in the folded ensemble of CaM's C-terminal domain present chemically and sterically distinct topologies that may facilitate conformational selection. Furthermore, we find that local unfolding is off-pathway for the exchange process relevant for peptide binding, in contrast to prior hypotheses that unfolding might account for binding diversity. Finally, our model predicts a novel binding interface that is well-populated in the Ca(2+)-bound regime and, thus, a candidate for pharmacological intervention." @default.
• W2337942016 created "2016-06-24" @default.
• W2337942016 creator A5032418986 @default.
• W2337942016 creator A5053940473 @default.
• W2337942016 creator A5077404353 @default.
• W2337942016 date "2016-04-04" @default.
• W2337942016 modified "2023-10-15" @default.
• W2337942016 title "Conformational heterogeneity of the calmodulin binding interface" @default.
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• W2337942016 doi "https://doi.org/10.1038/ncomms10910" @default.
• W2337942016 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4822001" @default.
• W2337942016 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27040077" @default.
• W2337942016 hasPublicationYear "2016" @default.
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