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Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops
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SYSNO ASEP 0541895 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops Author(s) Wosicki, S. (PL)
Kazmierczyk, M. (PL)
Gilski, M. (PL)
Zábranská, Helena (UOCHB-X) RID
Pichová, Iva (UOCHB-X) RID, ORCID
Jaskolski, M. (PL)Source Title Protein Science. - : Wiley - ISSN 0961-8368
Roč. 30, č. 6 (2021), s. 1258-1263Number of pages 6 s. Language eng - English Country US - United States Keywords active site architecture ; aspartic protease ; dimer ; flap structure ; inhibitor ; Mason‐Pfizer monkey virus ; M-PMV ; retropepsin ; retrovirus OECD category Biochemistry and molecular biology Method of publishing Open access Institutional support UOCHB-X - RVO:61388963 UT WOS 000637810000001 EID SCOPUS 85104043995 DOI 10.1002/pro.4072 Annotation 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. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2022 Electronic address https://doi.org/10.1002/pro.4072
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