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

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 sm...

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Detalles Bibliográficos
Autores principales: Wosicki, Stanislaw, Kazmierczyk, Maciej, Gilski, Miroslaw, Zabranska, Helena, Pichova, Iva, Jaskolski, Mariusz
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley & Sons, Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8138519/
https://www.ncbi.nlm.nih.gov/pubmed/33786913
http://dx.doi.org/10.1002/pro.4072
Descripción
Sumario: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 P2(1) crystal structures and is similar to a rarely occurring system in HIV‐1 PR.