Počet záznamů: 1

Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution

  1. 1.
    0369318 - UMCH-V 2012 RIV GB eng J - Článek v odborném periodiku
    Kolenko, Petr - Rozbeský, Daniel - Vaněk, Ondřej - Bezouška, Karel - Hašek, Jindřich - Dohnálek, Jan
    Structure of the H107R variant of the extracellular domain of mouse NKR-P1A at 2.3 Å resolution.
    Acta Crystallographica Section F. Roč. 67, č. 12 (2011), s. 1519-1523 ISSN 1744-3091
    Grant CEP: GA ČR GA305/07/1073; GA ČR GAP302/11/0855; GA MŠk 1M0505
    Výzkumný záměr: CEZ:AV0Z40500505; CEZ:AV0Z50200510; CEZ:AV0Z10100521
    Klíčová slova: NKR-P1A * merohedral twinning * mutation
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 0.506, rok: 2011

    The structure of the H107R variant of the extracellular domain of the mouse natural killer cell receptor NKR-P1A has been determined by X-ray diffraction at 2.3 A° resolution from a merohedrally twinned crystal. Unlike the structure of the wild-type receptor in space group I4122 with a single chain per asymmetric unit, the crystals of the variant belonged to space group I41 with a dimer in the asymmetric unit. Different degrees of merohedral twinning were detected in five data sets collected from different crystals. The mutation does not have a significant impact on the overall structure, but led to the binding of an additional phosphate ion at the interface of the molecules.
    Trvalý link: http://hdl.handle.net/11104/0203413