Veerapandian B, Gilliland G L, Raag R, Svensson A L, Masui Y, Hirai Y, Poulos T L
Center for Advanced Research in Biotechnology, University of Maryland, Rockville.
Proteins. 1992 Jan;12(1):10-23. doi: 10.1002/prot.340120103.
The molecular structure of interleukin-1 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 framework 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.
白细胞介素-1β是一种在多种疾病过程中发挥作用的激素样细胞因子,其分子结构已在2.0埃分辨率下确定,并精修至晶体学R因子为0.19。该分子的框架由12条呈现假三重对称的反平行β链组成。其中6条链构成一个β桶,极性残基集中在两端。三维结构分析,结合定点诱变以及生化和免疫学研究结果表明,β桶的核心发挥着重要的功能作用。桶一端的一大片带电荷残基被认为是白细胞介素-1与其受体相互作用的结合表面。