Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops

0541895 - ÚOCHB 2022 RIV US eng J - Článek v odborném periodiku
Wosicki, S. - Kazmierczyk, M. - Gilski, M. - Zábranská, Helena - Pichová, Iva - Jaskolski, M.
Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops.
Protein Science. Roč. 30, č. 6 (2021), s. 1258-1263. ISSN 0961-8368. E-ISSN 1469-896X
Institucionální podpora: RVO:61388963
Klíčová slova: active site architecture * aspartic protease * dimer * flap structure * inhibitor * Mason‐Pfizer monkey virus * M-PMV * retropepsin * retrovirus
Obor OECD: Biochemistry and molecular biology
Impakt faktor: 6.993, rok: 2021
Způsob publikování: Open access
https://doi.org/10.1002/pro.4072

Mason‐Pfizer monkey virus protease (PR) was crystallized in complex with two pepstatin‐based inhibitors in P1 space group. In both crystal structures, the extended flap loops that lock the inhibitor/substrate over the active site, are visible in the electron density either completely or with only small gaps, providing the first observation of the conformation of the flap loops in dimeric complex form of this retropepsin. The H‐bond network in the active site (with D26N mutation) differs from that reported for the P21 crystal structures and is similar to a rarely occurring system in HIV‐1 PR.
Trvalý link: http://hdl.handle.net/11104/0319391