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

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    0105299 - UMG-J 20043047 RIV GB eng J - Journal Article
    Brynda, Jiří - Řezáčová, Pavlína - Fábry, Milan - Hořejší, Magdalena - Štouračová, Renata - Souček, Milan - Hradilek, Martin - Konvalinka, Jan - Sedláček, Juraj
    Inhibitor binding at the protein interface in crystals of a HIV-1 protease complex.
    [Vazba inhibitoru na proteinové rozhraní v krystalu komplexu HIV-1 proteázy.]
    Acta Crystallographica Section D-Biological Crystallography. 11, D60, - (2004), s. 1943-1948. ISSN 0907-4449
    R&D Projects: GA MŠMT LN00B030
    Institutional research plan: CEZ:AV0Z5052915
    Keywords : HIV-1 protease * phenylnorstatine inhibitor * crystal packing
    Subject RIV: CE - Biochemistry
    Impact factor: 1.693, year: 2004

    Depending 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

    V závislosti na nadbytku ligandu využitého pro tvorbu komplexu tvoří HIV-proteáza v komplexu s novým fenylnorstatinovým inhibitorem krystalovou hexagonální (P6(1)) nebo ortorombickou (P2(1)2(1)) symetrii. Ortorombická forma vykazuje neobvyklou komplexnost složení krystalu: kromě jedné molekuly inhibitoru vázané na aktivní místo enzymu je druhá molekula inhibitoru vázána na vnější ligand na proteinovém rozhraní
    Permanent Link: http://hdl.handle.net/11104/0000162

     
     

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