
pmid: 27773637
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.
Conformational changes, Aging, Neoplasms, Humans, Sirtuins, Structure-based drug design, Modulators, Protein–protein interactions, Crystallography, X-Ray
Conformational changes, Aging, Neoplasms, Humans, Sirtuins, Structure-based drug design, Modulators, Protein–protein interactions, Crystallography, X-Ray
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
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