Multiple crystal forms of human MacroD2
Wazir, Sarah; Maksimainen, Mirko M.; Lehtiö, Lari (2020-10-31)
Wazir, S., Maksimainen, M. M., & Lehtiö, L. (2020). Multiple crystal forms of human MacroD2. Acta Crystallographica Section F Structural Biology Communications, 76(10), 477–482. https://doi.org/10.1107/s2053230x20011309
© 2020 International Union of Crystallography. The final authenticated version is available online at https://doi.org/10.1107/s2053230x20011309.
https://rightsstatements.org/vocab/InC/1.0/
https://urn.fi/URN:NBN:fi-fe2020120399311
Tiivistelmä
Abstract
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 Å 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.
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