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Crystal structure analysis of human Sirt2 and its ADP-ribose complex.

Title data

Moniot, Sébastien ; Schutkowski, Mike ; Steegborn, Clemens:
Crystal structure analysis of human Sirt2 and its ADP-ribose complex.
In: Journal of Structural Biology. Vol. 182 (May 2013) Issue 2 . - pp. 136-143.
ISSN 1047-8477

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Abstract in another language

Sirtuins are NAD(+)-dependent protein deacetylases that regulate metabolism and aging-related processes. Sirt2 is the only cytoplasmic isoform among the seven mamalian Sirtuins (Sirt1-7) and structural information concerning this isoform is limited. We crystallized Sirt2 in complex with a product analog, ADP-ribose, and solved this first crystal structure of a Sirt2 ligand complex at 2.3Å resolution. Additionally, we re-refined the structure of the Sirt2 apoform and analyzed the conformational changes associated with ligand binding to derive insights into the dynamics of the enzyme. Our analyses also provide information on Sirt2 peptide substrate binding and structural states of a Sirt2-specific protein region, and our insights and the novel Sirt2 crystal form provide helpful tools for the development of Sirt2 specific inhibitors.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 23454361
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Clemens Steegborn
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 20 Apr 2015 12:12
Last Modified: 20 Apr 2015 12:12
URI: https://eref.uni-bayreuth.de/id/eprint/10390