Počet záznamů: 1

Molecular architecture of mouse activating NKR-P1 receptors

  1. 1.
    0363604 - UMCH-V 2012 RIV US eng J - Článek v odborném periodiku
    Kolenko, Petr - Rozbeský, Daniel - Vaněk, Ondřej - Kopecký, V. Jr. - Hofbauerová, Kateřina - Novák, Petr - Pompach, Petr - Hašek, Jindřich - Skálová, Tereza - Bezouška, Karel - Dohnálek, Jan
    Molecular architecture of mouse activating NKR-P1 receptors.
    Journal of Structural Biology. Roč. 175, č. 3 (2011), s. 434-441 ISSN 1047-8477
    Grant CEP: GA MŠk 1M0505; GA ČR GA303/09/0477; GA ČR GD305/09/H008; GA ČR GA305/07/1073; GA ČR GAP207/10/1040; GA AV ČR KJB101120805
    Výzkumný záměr: CEZ:AV0Z40500505; CEZ:AV0Z50200510
    Klíčová slova: NK cell * C-type lectin-like receptor * X-ray structure
    Kód oboru RIV: CE - Biochemie
    Impakt faktor: 3.406, rok: 2011

    Receptors belonging to NKR-P1 family and their specific Clr ligands form an alternative missing self recognition system critical in immunity against tumors and viruses, elimination of tumor cells subjected to genotoxic stress, activation of T cell dependent immune response, and hypertension. The three-dimensional structure of the extracellular domain of the mouse natural killer (NK) cell receptor mNKR-P1Aex has been determined by X-ray diffraction. The core of the C-type lectin domain (CTLD) is homologous to the other CTLD receptors whereas one quarter of the domain forms an extended loop interacting tightly with a neighboring loop in the crystal. This domain swapping mechanism results in a compact interaction interface. A second dimerization interface resembles the known arrangement of other CTLD NK receptors. A functional dimeric form of the receptor is suggested, with the loop, evolutionarily conserved within this family, proposed to participate in interactions with ligands.
    Trvalý link: http://hdl.handle.net/11104/0199359