Nishimura C, Hanzawa H, Itoh S, Yasukawa K, Shimada I, Kishimoto T, Arata Y
Faculty of Pharmaceutical Sciences, University of Tokyo Bunkyo-ku, Japan.
Biochim Biophys Acta. 1990 Dec 5;1041(3):243-9. doi: 10.1016/0167-4838(90)90278-n.
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.
报道了人白细胞介素6（IL-6）中芳香族残基的¹H-NMR共振的部分归属。同核Hartmann-Hahn谱清楚地显示了IL-6中存在的组氨酸、酪氨酸和色氨酸残基的所有连接性。使用氘交换方法，已确定了His-16和His-165的咪唑质子共振。酪氨酸残基的碘化导致了Tyr-32的归属。光化学诱导动态核极化数据表明，His-16、Tyr-32和Trp-158暴露于溶剂中，而His-165、Tyr-98和Tyr-101则被埋藏。Tyr-32的碘化对IL-6活性没有显著影响，表明Tyr-32不负责IL-6的活性。
