CRYSTAL-STRUCTURE OF INTERLEUKIN-10 REVEALS AN INTERFERON GAMMA-LIKE FOLD

被引：127

作者：

WALTER, MR

NAGABHUSHAN, TL

机构：

[1] UNIV ALABAMA,CTR MACROMOLEC CRYSTALLOG,BIRMINGHAM,AL 35294

[2] SCHERING PLOUGH CORP,RES INST,KENILWORTH,NJ 07033

来源：

BIOCHEMISTRY | 1995年 / 34卷 / 38期

关键词：

D O I：

10.1021/bi00038a004

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：

The crystal structure of recombinant human interleukin 10 (rhIL-10) has been determined by X-ray crystallography at 2.0 Angstrom resolution. Interleukin 10 is a dimer composed of identical polypeptide chains related by a 2-fold axis. The molecule is predominantly alpha-helical. The main-chain fold resembles that of interferon gamma (IFN-gamma) in which the structural integrity of each domain is dependent on the intertwining of helices from each peptide chain. Comparison of rhIL-10 and IFN-gamma reveals differences in helix lengths and orientations of the 2-fold related domains. Interleukin 10 and IFN-gamma contain several conserved residues in their internal cores which suggest a possible ''fingerprint'' for detection of other members of this fold.

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页码：12118 / 12125

页数：8

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