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Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops
Author(s) -
Wosicki Stanislaw,
Kazmierczyk Maciej,
Gilski Miroslaw,
Zabranska Helena,
Pichova Iva,
Jaskolski Mariusz
Publication year - 2021
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.4072
Subject(s) - active site , crystal structure , pepstatin , crystallography , chemistry , stereochemistry , substrate (aquarium) , protease , biology , enzyme , biochemistry , ecology
Mason‐Pfizer monkey virus protease (PR) was crystallized in complex with two pepstatin‐based inhibitors in P 1 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 P 2 1 crystal structures and is similar to a rarely occurring system in HIV‐1 PR.