HIGH-RESOLUTION SOLUTION STRUCTURE OF THE BETA-CHEMOKINE HMIP-1-BETA BY MULTIDIMENSIONAL NMR
HIGH-RESOLUTION SOLUTION STRUCTURE OF THE BETA-CHEMOKINE HMIP-1-BETA BY MULTIDIMENSIONAL NMR
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DOI：
10.1126/science.8134838
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发表时间：
1994-03-25
期刊：
影响因子：
56.9
通讯作者：
CLORE, GM
中科院分区：
文献类型：
--
作者：
LODI, PJ;GARRETT, DS;CLORE, GM
趋化因子β亚家族成员——人巨噬细胞炎症蛋白-1β（hMIP-1β）的三维结构已通过溶液多维异核磁共振波谱法测定。人 MIP-1 β 是一种对称同源二聚体，相对分子质量约为 16 千道尔顿。 hMIP-1 β 单体的结构与相关的 α 趋化因子白细胞介素 8 (IL-8) 相似。然而，两种蛋白质的四级结构完全不同，二聚体界面由完全不同的残基组形成。 IL-8 二聚体是球形的，而 hMIP-1 β 二聚体是细长的圆柱形。这为α和β趋化因子亚家族之间不存在交叉结合和反应性提供了合理的解释。二聚化溶剂化自由能的计算表明，两种不同类型二聚体的形成和稳定是由疏水残基的掩埋引起的。
The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of similar to 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interfaceis formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.