High-resolution structure of a retroviral protease folded as a monomer
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F11%3A00369861" target="_blank" >RIV/61388963:_____/11:00369861 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1107/S0907444911035943" target="_blank" >http://dx.doi.org/10.1107/S0907444911035943</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S0907444911035943" target="_blank" >10.1107/S0907444911035943</a>
Alternative languages
Result language
angličtina
Original language name
High-resolution structure of a retroviral protease folded as a monomer
Original language description
Biophysical and NMR studies of M-PMV protease have indicated that in the absence of substrates or inhibitors M-PMV PR should fold into a stable monomer, but the crystal structure of this protein could not be solved by molecular replacement despite countless attempts. The solution was obtained in mr-rosetta using a model constructed by players of the game Foldit. The structure shows a monomeric protein, with the N- and C-termini completely disordered. The flap loop has an unusual curled shape and a different orientation from both the open and closed states known from dimeric retropepsins. This structure provides important information for the design of dimerization inhibitors of retroviral proteases.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
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Result continuities
Project
<a href="/en/project/1M0508" target="_blank" >1M0508: New Antivirals and Antineoplastics</a><br>
Continuities
Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Acta Crystallographica Section D-Biological Crystallography
ISSN
0907-4449
e-ISSN
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Volume of the periodical
D67
Issue of the periodical within the volume
11
Country of publishing house
DK - DENMARK
Number of pages
8
Pages from-to
907-914
UT code for WoS article
000296787400001
EID of the result in the Scopus database
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