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Statements

Subject Item
n2:RIV%2F68378050%3A_____%2F02%3A23033203%21RIV%2F2004%2FAV0%2FA23004%2FN
rdf:type
n6:Vysledek skos:Concept
dcterms:description
Crystallization conditions for an HIV-1 protease-inhibitor complwx were optimized to produce superior crystals for X-ray diffraction experiments. The X-ray structure of the HIV-1 protease complex was solved and regined at 1.16 A resoluton. In contrast to Saquinavir, the minetic hydroxy group of the inhibitor Z-Pns-Phe-Glu-Glu-NH2 is placed asymmetrically with respect to the non-ctystallographic twofold axis of the protease dimer so that hydrogen bonds between the carbonyl group of the inhibitor and the catalytic aspartates can be formed. The inhibitor binds in the centre of the active site by a compact network of hydrogen bonds to Gly1027, Gly2027, Asp 1025, Asp2025 and via the buried water molecule W7001 to lle 1050 and lle2050. Factors contributing to unusually high, 1.16 a, resolution (e.g. new crystal packing, binding of second molecule of Z-Pns-Phe-Glu-Glu-Nh2, etc.) will discussed. Crystallization conditions for an HIV-1 protease-inhibitor complwx were optimized to produce superior crystals for X-ray diffraction experiments. The X-ray structure of the HIV-1 protease complex was solved and regined at 1.16 A resoluton. In contrast to Saquinavir, the minetic hydroxy group of the inhibitor Z-Pns-Phe-Glu-Glu-NH2 is placed asymmetrically with respect to the non-ctystallographic twofold axis of the protease dimer so that hydrogen bonds between the carbonyl group of the inhibitor and the catalytic aspartates can be formed. The inhibitor binds in the centre of the active site by a compact network of hydrogen bonds to Gly1027, Gly2027, Asp 1025, Asp2025 and via the buried water molecule W7001 to lle 1050 and lle2050. Factors contributing to unusually high, 1.16 a, resolution (e.g. new crystal packing, binding of second molecule of Z-Pns-Phe-Glu-Glu-Nh2, etc.) will discussed.
dcterms:title
Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution. Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution.
skos:prefLabel
Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution. Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution.
skos:notation
RIV/68378050:_____/02:23033203!RIV/2004/AV0/A23004/N
n3:strany
X1-X5
n3:aktivita
n16:Z
n3:aktivity
Z(AV0Z4055905), Z(AV0Z5052915)
n3:dodaniDat
n9:2004
n3:domaciTvurceVysledku
n4:7774729 n4:6367593 n4:3843149 n4:6745725 n4:3524442
n3:druhVysledku
n8:D
n3:duvernostUdaju
n18:S
n3:entitaPredkladatele
n19:predkladatel
n3:idSjednocenehoVysledku
665473
n3:idVysledku
RIV/68378050:_____/02:23033203
n3:jazykVysledku
n7:eng
n3:klicovaSlova
Structure of a HIV-1; protease; Inhibitor complex
n3:klicoveSlovo
n12:Inhibitor%20complex n12:Structure%20of%20a%20HIV-1 n12:protease
n3:kontrolniKodProRIV
[C4911A6D3528]
n3:mistoKonaniAkce
Jena, Německo [DE]
n3:mistoVydani
Jena
n3:nazevZdroje
9th International Conference on the crystallization of Biological Macromolecules.
n3:obor
n13:EB
n3:pocetDomacichTvurcuVysledku
5
n3:pocetTvurcuVysledku
8
n3:pocetUcastnikuAkce
0
n3:pocetZahranicnichUcastnikuAkce
0
n3:rokUplatneniVysledku
n9:2002
n3:tvurceVysledku
Hradílek, Martin Fábry, Milan Štouračová, Renata Brynda, Jiří Řezáčová, Pavlína Souček, Milan Sedláček, Juraj Konvalinka, Jan
n3:typAkce
n15:WRD
n3:zahajeniAkce
2002-03-23+01:00
n3:zamer
n5:AV0Z4055905 n5:AV0Z5052915
s:numberOfPages
1
n10:hasPublisher
Jena