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RESEARCH PAPER / 2025-08-30

Mechanistic basis of N-terminal domain-mediated allostery in SIRT6: integrating molecular dynamics simulations and biochemical assays.

Haiyue Tang, Wenjie Ma, Guoyou Zhang, Jiacheng Wei, Jianyang Ao, Shaoyong Lu

Key Laboratory of Protection, Development and Utilization of Medicinal Resources in Liupanshan Area, Ministry of Education, Peptide & Protein Drug Research Center, School of Pharmacy, Ningxia Medical University, Yinchuan, 750004, China.Key Laboratory of Protection, Development and Utilization of Medicinal Resources in Liupanshan Area, Ministry of Education, Peptide & Protein Drug Research Center, School of Pharmacy, Ningxia Medical University, Yinchuan, 750004, China. · pubmed

Abstract

SIRT6, a pivotal member of the NAD

The following analysis is generated by AI and may contain errors. It is separate from the authors’ abstract and is not peer review.

Research summary

The paper claims to elucidate the mechanistic basis of allostery in SIRT6, which is implicated in metabolic regulation and DNA repair. Understanding SIRT6's role could provide insights into mechanisms of aging and longevity, making it relevant to the field.

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