Proton nuclear magnetic resonance study of human interleukin 6: chemical modifications and partial spectral assignments for the aromatic residues.
Partial assignments for the 1H-NMR resonances of the aromatic residues in human interleukin 6 (IL-6) are reported. The homonuclear Hartmann-Hahn spectrum clearly shows all connectivities for the histidine, tyrosine and tryptophan residues that exist in IL-6. Using a deuterium exchange method, the imidazole proton resonances of His-16 and His-165 have been assigned. Iodination of the tyrosine residues led to the assignment of Tyr-32. Photo-chemically induced dynamic nuclear polarization data have shown that His-16, Tyr-32 and Trp-158 are exposed to solvent, whereas His-165, Tyr-98 and Tyr-101 are buried. Iodination of Tyr-32 gave no significant effect on IL-6 activity, suggesting that Tyr-32 is not responsible for IL-6 activity.
Nishimura
C
C
Faculty of Pharmaceutical Sciences, University of Tokyo Bunkyo-ku, Japan.
Hanzawa
H
H
Itoh
S
S
Yasukawa
K
K
Shimada
I
I
Kishimoto
T
T
Arata
Y
Y
D001667:Binding, Competitive; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D015850:Interleukin-6 / Q000737:chemistry* / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy
D015850:Interleukin-6