Original title: A Phenylnorstatine Inhibitor Binding to HIV-1 Protease: Geometry, Protonation and Subsite-Pocket Interactions Analyzed at Atomic Resolution
Authors: Brynda, Jiří ; Řezáčová, Pavlína ; Fábry, Milan ; Hořejší, Magdalena ; Štouračová, Renata ; Sedláček, Juraj ; Souček, M. ; Hradílek, M. ; Lepšík, M. ; Konvalinka, J.
Document type: Papers
Conference/Event: Meeting of the Czech and Slovak structural biologists /3./, Nové hrady (CZ), 2004-03-11 / 2004-03-13
Year: 2003
Language: eng
Abstract: The x-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH2 has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibiot shows subnanomolar Ki values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance developoment. The structure displays a unique pattern of hydrogen bonding to the two catalytic aspartate residues. The high resolution permits to assess the donor/acceptor realtions of this hydrogen bonding and to indicate a proton shared by the two catalytic residues. Structural mechanism for the unimpaired ihnibition of the protease Val82Ala mutant is also suggested, based on energy calculations and analyses.
Keywords: atomic resolution; HIV protease; inhibitor
Project no.: CEZ:AV0Z5052915 (CEP), OE67/1 (CEP)
Funding provider: GA MŠk
Host item entry: Materials Structure in Chemistry, Biology, Physics and Technology, ISSN 1211-5894

Institution: Institute of Molecular Genetics AS ČR (web)
Document availability information: Fulltext is available at the institute of the Academy of Sciences.
Original record: http://hdl.handle.net/11104/0087428

Permalink: http://www.nusl.cz/ntk/nusl-28156


The record appears in these collections:
Research > Institutes ASCR > Institute of Molecular Genetics
Conference materials > Papers
 Record created 2011-07-01, last modified 2023-04-24


No fulltext
  • Export as DC, NUŠL, RIS
  • Share