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

Mikulecký, Pavel; Zahradník, Jiří; Kolenko, Petr; Černý, Jiří; Charnavets, Tatsiana; Kolářová, Lucie; Nečasová, Iva; Pham, Phuong Ngoc; Schneider, Bohdan

doi:https://dx.doi.org/10.1107/S2059798316012237

Number of the records: 1

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

1.

SYSNO ASEP	0465935
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity
Author(s)	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}
Source Title	Acta Crystallographica Section D-Structural Biology. - : Oxford Blackwell - ISSN 2059-7983 Roč. 72, č. 9 (2016), s. 1017-1025
Number of pages	9 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	interferon-gamma receptor 2 ; fibronectin type III domain ; class 2 cytokine receptors
Subject RIV	EB - Genetics ; Molecular Biology
R&D Projects	GA16-20507S GA ČR - Czech Science Foundation (CSF)
	ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
Institutional support	BTO-N - RVO:86652036
UT WOS	000383998200004
DOI	10.1107/S2059798316012237
Annotation	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.
Workplace	Institute of Biotechnology
Contact	Monika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
Year of Publishing	2017

Number of the records: 1