Thursday, August 15, 2013
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Crystal structures of sirtuin 1 (SIRT1), SIRT2 and SIRT3 bound to inhibitors
structures of sirtuins bound to inhibitors could guide the development of
compounds directed against specific sirtuins. Crystal structures of a SIRT1
inhibitor bound to SIRT1, SIRT3 or a bacterial Sirt2 showed the compound co-occupied
a conserved pocket alongside the enzyme's catalytic product, thereby
preventing product release. The co-crystal structures also showed no
structural differences between the conserved pockets of the three sirtuins
that could account for their differing binding affinities for the inhibitor.
Crystal structures of a SIRT3 inhibitor bound to SIRT3 showed the compound
simultaneously occupied the acetyllysine binding site and the conserved
pocket. Ongoing work includes using the structural data to develop specific
inhibitors of SIRT3.
Published online Aug. 15, 2013
available for partnering
Gertz, M. et al. Proc.
Natl. Acad. Sci. USA; published online July 9, 2013;
Nguyen, G.T.T. et al. Acta Crystallogr. D. Biol. Crystallogr.;
July 17, 2013;
Contact: Clemens Steegborn, University of Bayreuth,
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