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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Acta+Crystallogr+D+Struct+Biol
2016 ; 72
(Pt 9
): 1017-25
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Crystal structure of human interferon-? receptor 2 reveals the structural basis
for receptor specificity
#MMPMID27599734
Mikulecký P
; Zahradník J
; Kolenko P
; ?erný J
; Charnavets T
; Kolá?ová L
; Ne?asová I
; Pham PN
; Schneider B
Acta Crystallogr D Struct Biol
2016[Sep]; 72
(Pt 9
): 1017-25
PMID27599734
show ga
Interferon-? receptor 2 is a cell-surface receptor that is required for
interferon-? 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-?
receptor 2 (IFN?R2) was solved by molecular replacement at 1.8?Ĺ resolution.
Similar to other class 2 receptors, IFN?R2 has two fibronectin type III domains.
The characteristic structural features of IFN?R2 are concentrated in its
N-terminal domain: an extensive ?-cation motif of stacked residues KWRWRH, a
NAG-W-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-? and
receptor 1, the ligands of IFN?R2.