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首页> 外文期刊>Biochemistry >Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.
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Solution structure of the human CC chemokine 2: A monomeric representative of the CC chemokine subtype.

机译：人CC趋化因子2的溶液结构：CC趋化因子亚型的单体代表。

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摘要

HCC-2, a 66-amino acid residue human CC chemokine, was reported to induce chemotaxis on monocytes, T-lymphocytes, and eosinophils. The three-dimensional structure of HCC-2 has been determined by 1H nuclear magnetic resonance (NMR) spectroscopy and restrained molecular dynamics calculations on the basis of 871 experimental restraints. The structure is well-defined, exhibiting average root-mean-square deviations of 0.58 and 0.96 A for the backbone heavy atoms and all heavy atoms of residues 5-63, respectively. In contrast to most other chemokines, subtle structural differences impede dimer formation of HCC-2 in a concentration range of 0.1 microM to 2 mM. HCC-2, however, exhibits the same structural elements as the other chemokines, i.e., a triple-stranded antiparallel beta-sheet covered by an alpha-helix, showing that the chemokine fold is not influenced by quaternary interactions. Structural investigations with a HCC-2 mutant prove that a third additional disulfide bond present in wild-type HCC-2 is not necessary for maintaining the relative orientation of the helix and the beta-sheet.
机译：据报道，HCC-2是一种具有66个氨基酸残基的人CC趋化因子，可诱导单核细胞，T淋巴细胞和嗜酸性粒细胞趋化。 HCC-2的三维结构已通过1H核磁共振（NMR）光谱和基于871个实验约束的约束分子动力学计算确定。该结构是明确定义的，对残基5-63的主链重原子和所有重原子分别显示0.58和0.96 A的平均均方根偏差。与大多数其他趋化因子相反，在0.1 microM至2 mM的浓度范围内，细微的结构差异会阻止HCC-2的二聚体形成。但是，HCC-2具有与其他趋化因子相同的结构元素，即被α-螺旋覆盖的三链反平行β-折叠，表明趋化因子折叠不受四元相互作用的影响。用HCC-2突变体进行的结构研究证明，野生型HCC-2中存在的第三个额外的二硫键对于维持螺旋和β-折叠的相对方向不是必需的。

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