Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution.

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F02%3A23033203" target="_blank" >RIV/68378050:_____/02:23033203 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Structure of a HIV-1 Protease-Inhibitor Complex determined at 1.1A resolution.
Original language 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 toSaquinavir, 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 thecatalytic 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.
Czech name
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Czech description
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Publication year
2002
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Article name in the collection
9th International Conference on the crystallization of Biological Macromolecules.
ISBN
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ISSN
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e-ISSN
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Number of pages
1
Pages from-to
"X1"-"X5"
Publisher name
Jena
Place of publication
Jena
Event location
Jena, Německo [DE]
Event date
Mar 23, 2002
Type of event by nationality
WRD - Celosvětová akce
UT code for WoS article
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