Structural highlights
Function
[THIO_ECOLI] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Publication Abstract from PubMed
MacroD2 is one of the three human macrodomain proteins characterized by their protein-linked mono-ADP-ribosyl-hydrolyzing activity. MacroD2 is a single-domain protein that contains a deep ADP-ribose-binding groove. In this study, new crystallization conditions for MacroD2 were found and three crystal structures of human MacroD2 in the apo state were solved in space groups P41212, P43212 and P43, and refined at 1.75, 1.90 and 1.70 A resolution, respectively. Structural comparison of the apo crystal structures with the previously reported crystal structure of MacroD2 in complex with ADP-ribose revealed conformational changes in the side chains of Val101, Ile189 and Phe224 induced by the binding of ADP-ribose in the active site. These conformational variations may potentially facilitate design efforts of a MacroD2 inhibitor.
Multiple crystal forms of human MacroD2.,Wazir S, Maksimainen MM, Lehtio L Acta Crystallogr F Struct Biol Commun. 2020 Oct 1;76(Pt 10):477-482. doi:, 10.1107/S2053230X20011309. Epub 2020 Sep 15. PMID:33006575[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wazir S, Maksimainen MM, Lehtio L. Multiple crystal forms of human MacroD2. Acta Crystallogr F Struct Biol Commun. 2020 Oct 1;76(Pt 10):477-482. doi:, 10.1107/S2053230X20011309. Epub 2020 Sep 15. PMID:33006575 doi:http://dx.doi.org/10.1107/S2053230X20011309
