Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00454168" target="_blank" >RIV/61388963:_____/15:00454168 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/15:00454168
Result on the web
<a href="http://dx.doi.org/10.1107/S1399004715019392" target="_blank" >http://dx.doi.org/10.1107/S1399004715019392</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1107/S1399004715019392" target="_blank" >10.1107/S1399004715019392</a>
Alternative languages
Result language
angličtina
Original language name
Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis
Original language description
The virulence of the Candida pathogens is enhanced by the production of secreted aspartic proteases, which therefore represent possible targets for drug design. Here, the crystal structure of the secreted aspartic protease Sapp2p from Candida parapsilosis was determined. Sapp2p was isolated from its natural source and crystallized in complex with pepstatin A, a classical aspartic protease inhibitor. The atomic resolution of 0.83 angstrom allowed the protonation states of the active-site residues to be inferred. A detailed comparison of the structure of Sapp2p with the structure of Sapp1p, the most abundant C. parapsilosis secreted aspartic protease, was performed. The analysis, which included advanced quantum-chemical interaction-energy calculations, uncovered molecular details that allowed the experimentally observed equipotent inhibition of both isoenzymes by pepstatin A to be rationalized.
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/GA14-23022S" target="_blank" >GA14-23022S: Structural studies of aspartic protease from Candida parapsilosis as a tool for design of antimycotic compounds.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
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 Crystalloghraphy
ISSN
1399-0047
e-ISSN
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Volume of the periodical
71
Issue of the periodical within the volume
12
Country of publishing house
DK - DENMARK
Number of pages
11
Pages from-to
2494-2504
UT code for WoS article
000365773900012
EID of the result in the Scopus database
2-s2.0-84948798309