A RECEPTOR-BINDING PEPTIDE FROM HUMAN INTERLEUKIN-6 - ISOLATION AND A PROTON NUCLEAR-MAGNETIC-RESONANCE STUDY

被引：15

作者：

EKIDA, T

NISHIMURA, C

MASUDA, S

ITOH, S

SHIMADA, I

ARATA, Y

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,7-3-1 HONGO,BUNKYO KU,TOKYO 113,JAPAN

[2] TOSOH CORP,AYASE,KANAGAWA,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1992年 / 189卷 / 01期

关键词：

D O I：

10.1016/0006-291X(92)91546-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In order to locate the receptor-binding region of human interleukin-6 (IL-6), twelve peptide fragments were prepared by digestion of IL-6 with lysylendopeptidase. A significant activity of the receptor-binding was observed only for a peptide Ile88-Lys121, although the activity was estimated at 104-fold less than that of intact IL-6. Solution structure of the peptide Ile88-Lys121 was analyzed by using two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The results indicate the presence of α-helices in the regions Leu93-Phe106 and Glu110-Ser119. On the basis of the NMR data, we also prepared two peptides. Four-fold less binding activity than that of the peptide Ile88-Lys121 was observed for the peptide Ile88-Arg105, but no activity for the peptide Glu110-Lys121. These results suggest that the helical peptide Ile88-Arg105 composes a part of the receptor-binding region. © 1992.

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页码：211 / 220

页数：10

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