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

SYSNO ASEP	0465935
Druh ASEP	J - Článek v odborném periodiku
Zařazení RIV	J - Článek v odborném periodiku
Poddruh J	Článek ve WOS
Název	Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity
Tvůrce(i)	Mikulecký, Pavel (BTO-N)_RID Zahradník, Jiří (BTO-N) Kolenko, Petr (BTO-N)_{ORCID, RID} Černý, Jiří (BTO-N)_{RID, ORCID} Charnavets, Tatsiana (BTO-N) Kolářová, Lucie (BTO-N) Nečasová, Iva (BTO-N) Pham, Phuong Ngoc (BTO-N) Schneider, Bohdan (BTO-N)_{RID, ORCID}
Zdroj.dok.	Acta Crystallographica Section D-Structural Biology. - : Oxford Blackwell - ISSN 2059-7983 Roč. 72, č. 9 (2016), s. 1017-1025
Poč.str.	9 s.
Jazyk dok.	eng - angličtina
Země vyd.	GB - Velká Británie
Klíč. slova	interferon-gamma receptor 2 ; fibronectin type III domain ; class 2 cytokine receptors
Vědní obor RIV	EB - Genetika a molekulární biologie
CEP	GA16-20507S GA ČR - Grantová agentura ČR
	ED1.1.00/02.0109 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy
Institucionální podpora	BTO-N - RVO:86652036
UT WOS	000383998200004
DOI	10.1107/S2059798316012237
Anotace	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.
Pracoviště	Biotechnologický ústav
Kontakt	Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
Rok sběru	2017

Počet záznamů: 1