FUNCTIONAL IMPLICATIONS OF INTERLEUKIN-1-BETA BASED ON THE 3-DIMENSIONAL STRUCTURE

被引：85
作者：
VEERAPANDIAN, B
GILLILAND, GL
RAAG, R
SVENSSON, AL
MASUI, Y
HIRAI, Y
POULOS, TL
机构：
[1] NATL INST STAND & TECHNOL, ROCKVILLE, MD 20850 USA
[2] OTSUKA PHARMACEUT CO LTD, TOKUSHIMA 77101, JAPAN
来源：
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS | 1992年 / 12卷 / 01期
关键词：
CRYSTALLOGRAPHY; MOLECULAR ISOMORPHOUS REPLACEMENT; MOLECULAR DYNAMICS; REFINEMENT; INTERLEUKIN; SITE-DIRECTED MUTAGENESIS; RECEPTOR-BINDING SURFACE; EPITOPE;
D O I：
10.1002/prot.340120103
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 molecular structure of interleukin-l-beta, a hormone-like cytokine with roles in several disease processes, has been determined at 2.0 A resolution and refined to a crystallographic R-factor of 0.19. The frame-work of this molecule consists of 12 antiparallel beta-strands exhibiting pseudo-3-fold symmetry. Six of the strands make up a beta-barrel with polar residues concentrated at either end. Analysis of the three-dimensional structure, together with results from site-directed mutagenesis and biochemical and immunological studies, suggest that the core of the beta-barrel plays an important functional role. A large patch of charged residues on one end of the barrel is proposed as the binding surface with which IL-1 interacts with its receptor.
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页码：10 / 23
页数：14
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