HIGH-RESOLUTION 3-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1-BETA IN SOLUTION BY 3-DIMENSIONAL AND 4-DIMENSIONAL NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
HIGH-RESOLUTION 3-DIMENSIONAL STRUCTURE OF INTERLEUKIN-1-BETA IN SOLUTION BY 3-DIMENSIONAL AND 4-DIMENSIONAL NUCLEAR-MAGNETIC-RESONANCE SPECTROSCOPY
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DOI：
10.1021/bi00223a005
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发表时间：
1991-03-05
期刊：
影响因子：
2.9
通讯作者：
GRONENBORN, AM
中科院分区：
文献类型：
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作者：
CLORE, GM;WINGFIELD, PT;GRONENBORN, AM
白细胞介素1-β（IL-1-β），153个残基和17.4 kDa的蛋白质，它在免疫和炎症反应中起着核心作用的高分辨率三维溶液结构的测定，已确定由异源（C-13和N-15）三维和四维NMR光谱。该结构基于3146个实验约束，包括2780个距离和366个扭转角（phi、psi和chi-1）约束。计算总共32个模拟退火结构，并且关于平均坐标位置的原子RMS分布对于骨架原子为0.41 +/-0.04埃，对于所有原子为0.82 +/-0.04埃（不包括N-末端的残基1和C-末端的残基152和153，它们是部分无序的）。在具有小于或等于40%的表面可及性的内侧链的情况下，关于所有原子的平均坐标位置的原子RMS分布为0.49 +/-0.03埃。IL-1-β类似于四面体，由排列在三个假对称拓扑单元中的12-β-链组成，每个拓扑单元包含5条链。根据三维结构对IL-1-β突变数据的分析表明，IL-1受体在蛋白质表面上存在三个不同的结合位点。这表明，每三个免疫球蛋白结构域，其中包括细胞外部分的IL-1受体识别这些网站之一。
The determination of the high-resolution three-dimensional solution structure of interleukin 1-beta (IL-1-beta), a protein of 153 residues and 17.4 kDa, which plays a central role in the immune and inflammatory responses, has been determined by heteronuclear (C-13 and N-15) three- and four-dimensional NMR spectroscopy. The structure is based on 3146 experimental restraints comprising 2780 distance and 366 torsion angle (phi, psi, and chi-1) restraints. A total of 32 simulated annealing structures are calculated, and the atomic RMS distribution about the mean coordinate positions is 0.41 +/- 0.04 angstrom for the backbone atoms and 0.82 +/- 0.04 angstrom for all atoms (excluding residue 1 at the N-terminus and residues 152 and 153 at the C-terminus, which are partially disordered). In the case of internal side chains with a surface accessibility of less-than-or-equal-to 40%, the atomic RMS distribution about the mean coordinate positions for all atoms is 0.49 +/- 0.03 angstrom. IL-1-beta resembles a tetrahedron and is composed of 12-beta-strands arranged in three pseudosymmetric topological units, each of which comprises 5 strands. Analysis of the mutational data on IL-1-beta in the light of the three-dimensional structure suggests the presence of three distinct binding sites for the IL-1 receptor on the surface of the protein. It is suggested that each of the three immunoglobulin domains which comprise the extracellular portion of the IL-1 receptor recognizes one of these sites.