Prediction and confirmation of a switch-like region within the N-terminal domain of hSIRT1.

ABSTRACT: Many proteins display conformational changes resulting from allosteric regulation. Often only a few residues are crucial in conveying these structural and functional allosteric changes. These regions that undergo a significant change in structure upon receiving an input signal, such as molecular recognition, are defined as switch-like regions. Identifying these key residues within switch-like regions can help elucidate the mechanism of allosteric regulation and provide guidance for synthetic regulation. In this study, we combine a novel computational workflow with biochemical methods to identify a switch-like region in the N-terminal domain of human SIRT1 (hSIRT1), a lysine deacetylase that plays important roles in regulating cellular pathways. Based on primary sequence, computational meth

SUBMITTER: Huynh AT 

PROVIDER: S-EPMC9112024 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature