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- W3014597124 endingPage "112365" @default.
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- W3014597124 abstract "Mutation (p.LEU112PRO) in carotenoid cleavage dioxygenase 8 (CCD8) protein increases tiller formation in rice plants by cross-talking with auxin and cytokinins. However, owing to the nonexistence of a three-dimension structure of CCD8, detail information about its structure and function remain elusive until date. Hence, in the present study, computational approaches were adopted to predict three-dimensional (3D) structure of CCD8 protein through comparative modeling techniques and to study the effect of mutation (p.LEU112PRO) on its function as well as architecture through molecular dynamics simulation studies. The obtained result reveals that wild-type CCD8 protein is made up of 10 α-helix and 25 β-strands while mutant CCD8 is made up of 11 α-helix and 24 β-strands. Further, molecular docking studies reveals that the wild-type has a better binding affinity with auxin and cytokinin in comparison to mutant. Subsequent molecular dynamics simulation of these four complexes, separately, reveals that the movement of both wild-type as well as mutant CCD8 get reduced after binding with auxin, which in turn prevent auxin transport out of the bud and increases tiller number. However, when cytokinin binds with wild-type and mutant CCD8, it inhibits and enhance CCD8 activity, respectively. As cytokinin positively regulates tiller number formation, enhance activity of mutant CCD8 after binding with cytokinin might be the main reason for more tiller number in mutant than wild-type plant. In the near future, mutant CCD8 along with auxin and cytokinin may be utilized for increasing grain yield in rice plants." @default.
- W3014597124 created "2020-04-10" @default.
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- W3014597124 date "2020-07-01" @default.
- W3014597124 modified "2023-10-14" @default.
- W3014597124 title "In silico characterization of the impact of mutation (LEU112PRO) on the structure and function of carotenoid cleavage dioxygenase 8 in Oryza sativa" @default.
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- W3014597124 doi "https://doi.org/10.1016/j.phytochem.2020.112365" @default.
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