Number of the records: 1  

Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex

  1. 1.
    SYSNO ASEP0105299
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JOstatní články
    TitleInhibitor binding at the protein interface in crystals of a HIV-1 protease complex
    TitleVazba inhibitoru na proteinové rozhraní v krystalu komplexu HIV-1 proteázy
    Author(s) Brynda, Jiří (UMG-J) RID
    Řezáčová, Pavlína (UMG-J) RID
    Fábry, Milan (UMG-J) RID
    Hořejší, Magdalena (UMG-J)
    Štouračová, Renata (UMG-J)
    Souček, Milan (UOCHB-X)
    Hradilek, Martin (UOCHB-X) ORCID
    Konvalinka, Jan (UOCHB-X) RID, ORCID
    Sedláček, Juraj (UMG-J) RID
    Source TitleActa Crystallographica Section D-Biological Crystallography. - : WILEY-BLACKWELL - ISSN 0907-4449
    11, D60, - (2004), s. 1943-1948
    Number of pages6 s.
    Languageeng - English
    CountryGB - United Kingdom
    KeywordsHIV-1 protease ; phenylnorstatine inhibitor ; crystal packing
    Subject RIVCE - Biochemistry
    R&D ProjectsLN00B030 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    CEZAV0Z5052915 - UMG-J
    AnnotationDepending on the excess of ligand used for complex formation, the HIV-protease complexed with a novel phenylnorstatine inhibitor forms crystal either hexagonal (P6(1)) or orthorhombic (P2(1)2(1)) symetry. The orthorhombic form shows an unusual complexity of crystal packing: in addition to one inhibitor molecule that is bound to the enzyme active site, the second inhibitor molecule is bound as an outer ligand at the protein interface
    WorkplaceInstitute of Molecular Genetics
    ContactNikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217
    Year of Publishing2005

Number of the records: 1  

Metadata are licenced under CC0

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.