Human sirtuins: Structures and flexibility.
- Sacconnay L School of Pharmaceutical Sciences, University of Geneva, University of Lausanne, Rue Michel Servet 1, CH-1211 Geneva 4, Switzerland.
- Carrupt PA School of Pharmaceutical Sciences, University of Geneva, University of Lausanne, Rue Michel Servet 1, CH-1211 Geneva 4, Switzerland.
- Nurisso A School of Pharmaceutical Sciences, University of Geneva, University of Lausanne, Rue Michel Servet 1, CH-1211 Geneva 4, Switzerland; Département de Biochimie, Université de Montréal, H3C 3J7 Montréal, Québec, Canada.
- 2016-10-30
Published in:
- Journal of structural biology. - 2016
Conformational changes
Modulators
Protein–protein interactions
Sirtuins
Structure-based drug design
Aging
Crystallography, X-Ray
Humans
Neoplasms
Sirtuins
English
In recent years, sirtuins (SIRTs), members of histone deacetylases (HDACs) class III, have been found to modulate cellular processes related to the development of human aging-related pathologies (i.e. cancer, neurodegeneration, metabolic disorders). Several crystallographic structures and computational studies have shed light into their catalytic mechanism of action, identifying also the structural elements for the design of selective drug candidates. In this review, we first aim at summarizing the structural features characterizing human SIRTs. We then describe the observed mass and one-off movements related to conformational changes upon SIRT-mediated recognition events. Such information will be useful not only for rationalizing the design of new SIRT modulators, but also for improving the comprehension of SIRT-related biological roles.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/j.jsb.2016.10.008
- PMID 27773637
- Persistent URL
- https://sonar.ch/global/documents/213660
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