The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F12%3A00376528" target="_blank" >RIV/61388963:_____/12:00376528 - isvavai.cz</a>

Alternative codes found

RIV/68378050:_____/12:00376528

Result on the web

<a href="http://dx.doi.org/10.3109/14756366.2011.627508" target="_blank" >http://dx.doi.org/10.3109/14756366.2011.627508</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.3109/14756366.2011.627508" target="_blank" >10.3109/14756366.2011.627508</a>

Result language

angličtina

Original language name

The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir

Original language description

Secreted aspartic proteases (Saps) are extracellular proteolytic enzymes that enhance the virulence of Candida pathogens. These enzymes therefore represent possible targets for therapeutic drug design. Saps are inhibited by nanomolar concentrations of the classical inhibitor of aspartic proteases pepstatin A and also by the inhibitors of the HIV protease, but with the K-i of micromolar values or higher. To contribute to the discussion regarding whether HIV protease inhibitors can act against opportunistic mycoses by the inhibition of Saps, we determined the structure of Sapp1p from Candida parapsilosis in complex with ritonavir (RTV), a clinically used inhibitor of the HIV protease. The crystal structure refined at resolution 2.4 angstrom proved binding of RTV into the active site of Sapp1p and provided the structural information necessary to evaluate the stability and specificity of the protein-inhibitor interaction.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year

2012

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Enzyme Inhibition and Medicinal Chemistry

ISSN

1475-6366

e-ISSN

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Volume of the periodical

27

Issue of the periodical within the volume

1

Country of publishing house

GB - UNITED KINGDOM

Number of pages

6

Pages from-to

160-165

UT code for WoS article

000298748800024

EID of the result in the Scopus database

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