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学科主题: 生命有机化学
题名: Solution structure and dynamics of human metallothionein-3 (MT-3) zinc
其他题名: 人金属硫蛋白 MT3的溶液结构和动力学
作者: Wang H(王辉) ; Zhang Q(张琪) ; Cai B(蔡斌) ; Li HY(李红燕) ; Kong-Hung Sze ; Huang ZX(黄仲贤) ; Wu HM(吴厚铭) ; SUN HONGZHE
通讯作者: 吴厚铭 ; SUN HONGZHE
刊名: FEBS Lett.
发表日期: 2006-01-01
卷: 580, 期:3, 页:795-800
收录类别: SCI
部门归属: 香港大学化学系与化学生物性开放实验室; 上海有机化学研究所生命有机化学国家重点实验室; 复旦大学化学系
英文摘要: Alzheimer's disease is characterized by progressive loss of neurons accompanied by the formation of intraneural neurofibrillary tangles and extracellular amyloid plaques. Human neuronal growth inhibitory factor, classified as metallothionein-3 (MT-3), was found to be related to the neurotrophic activity promoting cortical neuron survival and dendrite outgrowth in the cell culture studies. We have determined the solution structure of the a-domain of human MT-3 (residues 32-68) by multinuclear and multidimensional NMR spectroscopy in combination with the molecular dynamic simulated annealing approach. The human MT-3 shows two metal-thiolate clusters, one in the N-terminus (beta-domain) and one in the C-terminus (alpha-domain). The overall fold of the alpha-domain is similar to that of mouse MT-3. However, human MT-3 has a longer loop in the acidic hexapeptide insertion than that of mouse MT-3. Surprisingly, the backbone dynamics of the protein revealed that the beta-domain exhibits similar internal motion to the alpha-domain, although the N-terminal residues are more flexible. Our results may provide useful information for understanding the structure-function relationship of human MT-3. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
语种: 英语
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内容类型: 期刊论文
URI标识: http://ir.sioc.ac.cn/handle/331003/17373
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
Wang H,Zhang Q,Cai B,et al. Solution structure and dynamics of human metallothionein-3 (MT-3) zinc[J]. FEBS Lett.,2006,580(3):795-800.
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