Three-dimensional structure of recombinant human interferon-gamma.
The x-ray crystal structure of recombinant human interferon-gamma has been determined with the use of multiple-isomorphous-replacement techniques. Interferon-gamma, which is dimeric in solution, crystallizes with two dimers related by a noncrystallographic twofold axis in the asymmetric unit. The protein is primarily alpha helical, with six helices in each subunit that comprise approximately 62 percent of the structure; there is no beta sheet. The dimeric structure of human interferon-gamma is stabilized by the intertwining of helices across the subunit interface with multiple intersubunit interactions.
Ealick
S E
SE
Department of Pharmacology, University of Alabama, Birmingham 35294.
Cook
W J
WJ
Vijay-Kumar
S
S
Carson
M
M
Nagabhushan
T L
TL
Trotta
P P
PP
Bugg
C E
CE
D000595:Amino Acid Sequence; D003460:Crystallization; D006031:Glycosylation; D006801:Humans; D007371:Interferon-gamma / Q000737:chemistry*; D046911:Macromolecular Substances; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D011994:Recombinant Proteins; D007371:Interferon-gamma