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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F12%3A00376528%21RIV13-GA0-68378050
rdf:type
skos:Concept n18:Vysledek
dcterms: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. 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.
dcterms:title
The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir
skos:prefLabel
The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir The crystal structure of protease Sapp1p from Candida parapsilosis in complex with the HIV protease inhibitor ritonavir
skos:notation
RIV/68378050:_____/12:00376528!RIV13-GA0-68378050
n18:predkladatel
n19:ico%3A68378050
n4:aktivita
n5:P n5:Z
n4:aktivity
P(GA203/09/0820), P(GA310/09/1945), P(LC531), Z(AV0Z40550506), Z(AV0Z50520514)
n4:cisloPeriodika
1
n4:dodaniDat
n12:2013
n4:domaciTvurceVysledku
n17:2204908
n4:druhVysledku
n6:J
n4:duvernostUdaju
n11:S
n4:entitaPredkladatele
n13:predkladatel
n4:idSjednocenehoVysledku
129126
n4:idVysledku
RIV/68378050:_____/12:00376528
n4:jazykVysledku
n15:eng
n4:klicovaSlova
secreted aspartic protease; virulence factor; X-ray structure; candidiasis
n4:klicoveSlovo
n7:candidiasis n7:secreted%20aspartic%20protease n7:X-ray%20structure n7:virulence%20factor
n4:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n4:kontrolniKodProRIV
[7ADD7166D1E4]
n4:nazevZdroje
Journal of Enzyme Inhibition and Medicinal Chemistry
n4:obor
n16:CE
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
6
n4:projekt
n9:GA203%2F09%2F0820 n9:GA310%2F09%2F1945 n9:LC531
n4:rokUplatneniVysledku
n12:2012
n4:svazekPeriodika
27
n4:tvurceVysledku
Brynda, Jiří Pachl, Petr Řezáčová, Pavlína Dostál, Jiří Hrušková, Olga Pichová, Iva
n4:wos
000298748800024
n4:zamer
n14:AV0Z40550506 n14:AV0Z50520514
s:issn
1475-6366
s:numberOfPages
6
n20:doi
10.3109/14756366.2011.627508