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学科主题: 生命有机化学
题名: NMR solution structure of BmK-beta IT, an excitatory scorpion beta-toxin without a 'hot spot' at the relevant position structure
其他题名: BmK-bIT, 一个在重要位置没有“热点”的激动型蝎毒素的NMR溶液结构
作者: Tong XT(童孝田) ; Yao J(姚镜) ; He FH(何发虎) ; Chen X(陈翔) ; Zheng XH(郑训海) ; Xie C(谢昌) ; Wu G(吴宫) ; Zhang NX(张乃霞) ; Ding JP(丁久平) ; Wu HM(吴厚铭)
通讯作者: 吴厚铭
刊名: Biochem. Biophys. Res. Commun.
发表日期: 2006-01-01
卷: 349, 期:3, 页:890-899
收录类别: SCI
部门归属: 上海有机化学研究所生命有机化学国家重点实验室; 华中理工大学生物化学与生物物理研究所
英文摘要: BmK-beta IT (previously named as Bm32-VI in the literature), an excitatory scorpion beta-toxin, is purified from the venom of the Chinese scorpion Buthus martensii Karsch. it features a primary sequence typical of the excitatory anti-insect toxins: two contiguous Cys residues (Cys37-Cys38) and a shifted location of the fourth disulfide bridges (Cys38-Cys64), and demonstrates bioactivity characteristic of the excitatory beta-toxins. However, it is noteworthy that BmK-beta IT is not conserved with a glutamate residue at the preceding position of the third Cys residue, and is the first example having a non-glutamate residue at the relevant position in the excitatory scorpion beta-toxin subfamily. The 3D structure of BmK-beta IT is determined with 2D NMR spectroscopy and molecular modeling. The solution structure of BmK-beta IT is closely similar to those of BmK MAP and Bj-xtrIT, only distinct from the latter by lack of an alpha(0)-helix. The surface functional patch comparison with those of BmK IT-AP and Bj-xtrIT reveals their striking similarity in the spatial arrangement. These results infer that the functional surface of beta-toxins is composed of two binding regions and a functional site. The main binding site is consisted of hydrophobic residues surrounding the alpha(1)-helix and its preceding loop, which is common to all beta-type scorpion toxins affecting Na+ channels. The second binding site, which determines the specificity of the toxin, locates at the C-terminus for excitatory insect beta-toxin, while rests at the beta-sheet and its linking loop for anti-mammal toxins. The functional site involved in the voltage sensor-trapping model, which characterizes the function of all beta-toxins, is the negatively charged residue Glu15. (c) 2006 Elsevier Inc. 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/331003/17367
Appears in Collections:上海有机化学研究所_期刊论文

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Recommended Citation:
Tong XT,Yao J,He FH,et al. NMR solution structure of BmK-beta IT, an excitatory scorpion beta-toxin without a 'hot spot' at the relevant position structure[J]. Biochem. Biophys. Res. Commun.,2006,349(3):890-899.
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