期刊
SCIENTIFIC REPORTS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41598-019-47063-1
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资金
- Yokohama City University
Calmodulin is a calcium binding protein with two lobes, N-lobe and C-lobe, which evolved from duplication and fusion of a single precursor lobe of a pair of EF-hand. These two lobes of calmodulin show subtle differences in calcium binding and target recognition; these are important for the functions of calmodulin. Since the structures, especially main chain conformations, of two EF-lobes in holo-form are quite similar; this is a good example to evaluate the effect of side chains for structural dynamics. We analyzed the structure of calmodulin using molecular dynamics and found differences in conformational ensembles between N- and C-lobes. We also showed the mutant structures created by homology modeling could reproduce the difference of dynamic motion between N-and C-lobes.
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