Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00541895" target="_blank" >RIV/61388963:_____/21:00541895 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1002/pro.4072" target="_blank" >https://doi.org/10.1002/pro.4072</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/pro.4072" target="_blank" >10.1002/pro.4072</a>
Alternative languages
Result language
angličtina
Original language name
Crystal structures of inhibitor complexes of M‐PMV protease with visible flap loops
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Science
ISSN
0961-8368
e-ISSN
1469-896X
Volume of the periodical
30
Issue of the periodical within the volume
6
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
1258-1263
UT code for WoS article
000637810000001
EID of the result in the Scopus database
2-s2.0-85104043995