Počet záznamů: 1  

Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity

  1. 1.
    0465935 - BTO-N 2017 RIV GB eng J - Článek v odborném periodiku
    Mikulecký, Pavel - Zahradník, Jiří - Kolenko, Petr - Černý, Jiří - Charnavets, Tatsiana - Kolářová, Lucie - Nečasová, Iva - Pham, Phuong Ngoc - Schneider, Bohdan
    Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity.
    Acta Crystallographica Section D-Structural Biology. Roč. 72, č. 9 (2016), s. 1017-1025. ISSN 2059-7983
    Grant CEP: GA ČR(CZ) GA16-20507S; GA MŠk(CZ) ED1.1.00/02.0109
    Institucionální podpora: RVO:86652036
    Klíčová slova: interferon-gamma receptor 2 * fibronectin type III domain * class 2 cytokine receptors
    Kód oboru RIV: EB - Genetika a molekulární biologie
    Impakt faktor: 2.114, rok: 2016

    Interferon-gamma receptor 2 is a cell-surface receptor that is required for interferon-gamma signalling and therefore plays a critical immunoregulatory role in innate and adaptive immunity against viral and also bacterial and protozoal infections. A crystal structure of the extracellular part of human interferon-gamma receptor 2 (IFN gamma R2) was solved by molecular replacement at 1.8 angstrom resolution. Similar to other class 2 receptors, IFN gamma R2 has two fibronectin type III domains. The characteristic structural features of IFN gamma R2 are concentrated in its N-terminal domain: an extensive pi-cation motif of stacked residues KWRWRH, a NAGW-NAG sandwich ( where NAG stands for N-acetyl-d-glucosamine) and finally a helix formed by residues 78-85, which is unique among class 2 receptors. Mass spectrometry and mutational analyses showed the importance of N-linked glycosylation to the stability of the protein and confirmed the presence of two disulfide bonds. Structure-based bioinformatic analysis revealed independent evolutionary behaviour of both receptor domains and, together with multiple sequence alignment, identified putative binding sites for interferon-gamma and receptor 1, the ligands of IFN gamma R2.
    Trvalý link: http://hdl.handle.net/11104/0264402