Ontology highlight
ABSTRACT:
SUBMITTER: Rumpf T
PROVIDER: S-EPMC4339887 | biostudies-literature | 2015 Feb
REPOSITORIES: biostudies-literature
Rumpf Tobias T Schiedel Matthias M Karaman Berin B Roessler Claudia C North Brian J BJ Lehotzky Attila A Oláh Judit J Ladwein Kathrin I KI Schmidtkunz Karin K Gajer Markus M Pannek Martin M Steegborn Clemens C Sinclair David A DA Gerhardt Stefan S Ovádi Judit J Schutkowski Mike M Sippl Wolfgang W Einsle Oliver O Jung Manfred M
Nature communications 20150212
Sirtuins are a highly conserved class of NAD(+)-dependent lysine deacylases. The human isotype Sirt2 has been implicated in the pathogenesis of cancer, inflammation and neurodegeneration, which makes the modulation of Sirt2 activity a promising strategy for pharmaceutical intervention. A rational basis for the development of optimized Sirt2 inhibitors is lacking so far. Here we present high-resolution structures of human Sirt2 in complex with highly selective drug-like inhibitors that show a uni ...[more]