ArticleFrontiers in bioinformatics2026
Elucidating binding hot spots and structural stability in sirtuin family proteins for selective inhibitors: a computational approach.
Article in Frontiers in bioinformatics, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Background: The sirtuin (SIRT) family is an NAD Methods: The workflow of our study included molecular docking and molecular dynamics studies to deeply explore conformational dynamics and binding hot spots selective to each SIRT isoform. Results: As an outcome of our study, we predicted the major flexible regions in each isoform, which may turn out to be selective for each SIRT isoform. Additionally, we predicted SIRT isoform-selective key residues that may regulate the inhibitory potential of SIRT proteins. The primary SIRT isoform-selective residues for SIRT1 were Phe273, Phe297, Tyr280, and His363; for SIRT2, they were Phe119, His187, Val233, Phe235, and Leu239; for SIRT3, they were Leu248, Glu296, and Arg301; for SIRT5, they were Phe70, Tyr102, Gln140, and His158; and for SIRT6, they were Asp61, Trp69, His131, Trp186, Ser214, Arg218, and Leu239. Conclusion: In this study, we provided a deep cognizance of SIRT biology and a fruitful initiative for
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