Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor.
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.
Walter
M R
MR
Department of Pharmacology, University of Alabama at Birmingham 35294, USA.
Windsor
W T
WT
Nagabhushan
T L
TL
Lundell
D J
DJ
Lunn
C A
CA
Zauodny
P J
PJ
Narula
S K
SK
D003196:Computer Graphics; D018360:Crystallography, X-Ray; D016207:Cytokines / Q000737:chemistry; D004926:Escherichia coli; D006031:Glycosylation; D013006:Growth Hormone / Q000737:chemistry; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry*; D011487:Protein Conformation; D017471:Receptors, Interferon / Q000737:chemistry*; D011986:Receptors, Somatotropin / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry; D012995:Solubility; D000096743:Interferon gamma Receptor
D016207:Cytokines; D013006:Growth Hormone; D007371:Interferon-gamma; D017471:Receptors, Interferon; D011986:Receptors, Somatotropin; D011994:Recombinant Proteins; D000096743:Interferon gamma Receptor