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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F86652036%3A_____%2F16%3A00465935" target="_blank" >RIV/86652036:_____/16:00465935 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1107/S2059798316012237" target="_blank" >http://dx.doi.org/10.1107/S2059798316012237</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1107/S2059798316012237" target="_blank" >10.1107/S2059798316012237</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2016

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Acta Crystallographica Section D-Structural Biology

ISSN

2059-7983

e-ISSN

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Svazek periodika

72

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

1017-1025

Kód UT WoS článku

000383998200004

EID výsledku v databázi Scopus

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