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• W4289745822 abstract "The introduction of CRISPR/Cas9 based gene editing has greatly accelerated therapeutic genome editing. However, the off-target DNA cleavage by CRISPR/Cas9 protein hampers its clinical translation, hindering its widespread use as a programmable genome editing tool. Although Cas9 variants with better mismatch discrimination have been developed, they have significantly lower rates of on-target DNA cleavage. Here, we have compared the dynamics of a more specific naturally occurring Cas9 from Francisella novicida (FnCas9) to the most widely used, SpCas9 protein. Long-scale atomistic MD simulation of free and gRNA bound forms of both the Cas9 proteins was performed, and their domain rearrangements and binding affinity with gRNA were compared to decipher the possible reason behind the enhanced specificity of FnCas9 protein. The greater binding affinity with gRNA, high domain electrostatics, and more volatility of FnCas9 than SpCas9 may explain its increased specificity and lower tolerance for mismatches." @default.
• W4289745822 created "2022-08-04" @default.
• W4289745822 creator A5041908980 @default.
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• W4289745822 date "2022-01-01" @default.
• W4289745822 modified "2023-09-25" @default.
• W4289745822 title "Comparative structural and dynamics study of free and gRNA-bound FnCas9 and SpCas9 proteins" @default.
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• W4289745822 doi "https://doi.org/10.1016/j.csbj.2022.07.041" @default.
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