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PMID: 7617032 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor.

Nature ·Vol. 376 ·No. 6537 ·1995-07-20 ·Pages 230-5

Walter MR, Windsor WT, Nagabhushan TL, Lundell DJ, Lunn CA, Zauodny PJ, Narula SK

Abstract

The crystal structure of interferon-gamma bound to the extracellular fragment of its high-affinity cell-surface receptor reveals the first view of a class-2 cytokine receptor-ligand complex. In the complex, one interferon-gamma homodimer binds two receptor molecules. Unlike the class-1 growth hormone receptor complex, the two interferon-gamma receptors do not interact with one another and are separated by 27 A. Upon receptor binding, the flexible AB loop of interferon-gamma undergoes a conformational change that includes the formation of a 3(10) helix.

MeSH Terms
Computer Graphics Crystallography, X-Ray Cytokines/chemistry Escherichia coli Glycosylation Growth Hormone/chemistry Humans Interferon-gamma/chemistry Protein Conformation Receptors, Interferon/chemistry Receptors, Somatotropin/chemistry Recombinant Proteins/chemistry Solubility
Chemicals
Cytokines Receptors, Interferon Receptors, Somatotropin Recombinant Proteins interferon gamma receptor Interferon-gamma Growth Hormone
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Walter M R
Department of Pharmacology, University of Alabama at Birmingham 35294, USA.
Windsor W T
Nagabhushan T L
Lundell D J
Lunn C A
Zauodny P J
Narula S K
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-07-20
Pages
230-5
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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