Solution structure of BmKK2, a new potassium channel blocker from the venom of Chinese scorpion Buthus martensi Karsch
文献类型：期刊论文
| 作者 | Zhang, NX ; Li, MH; Chen, X; Wang, Y; Wu, G; Hu, GY; Wu, HM
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| 刊名 | PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
 |
| 出版日期 | 2004-06-01 |
| 卷号 | 55期号:4页码:835-845 |
| 关键词 | BmKK2 Buthus martensi Karsch scorpion toxin NMR solution structure potassium channel blocker rSK channel Kv channel |
| ISSN号 | 0887-3585 |
| DOI | 10.1002/prot.20117 |
| 文献子类 | Article |
| 英文摘要 | A natural K+ channel blocker, BmKK2 (a member of scorpion toxin subfamily alpha-KTx 14), which is composed of 31 amino acid residues and purified from the venom of the Chinese scorpion Buthus martensi Karsch, was characterized using whole-cell patch-clamp recording in rat hippocampal neurons. The three dimensional structure of BmKK2 was determined with two-dimensional NMR spectroscopy and molecular modelling techniques. In solution this toxin adopted a common alpha/beta-motif, but showed distinct local conformation in the loop between alpha-helix and beta-sheet in comparison with typical short-chain scorpion toxins (e.g., CTX and NTX). Also, the a helix is shorter and the P-sheet element is smaller (each strand consisted only two residues). The unusual structural feature of BmKK2 was attributed to the shorter loop between the a-helix and P-sheet and the presence of two consecutive Pro residues at position 21 and 22 in the loop. Moreover, two models of BmKK2/hKv1.3 channel and BmKK2/rSK2 channel complexes were simulated with docking calculations. The results demonstrated the existence of a a-mode binding between the toxin and the channels. The model of BmKK rSK2 channel complex exhibited favorable contacts both in electrostatic and hydrophobic, including a network of five hydrogen bonds and bigger interface containing seven pairs of inter-residue interactions. In contrast, the model of BmKK2/hKv1.3 channel complex, containing only three pairs of interresidue interactions, exhibited poor contacts and smaller interface. The results well explained its lower activity towards Kv channel, and predicted that it may prefer a type of SK channel with a narrower entryway as its specific receptor. (C) 2004 Wiley-Liss, Inc. |
| WOS关键词 | MAGNETIC-RESONANCE DATA ; SHAKER K+ CHANNEL ; PANDINUS IMPERATOR ; PROTEIN STRUCTURES ; SMALL-CONDUCTANCE ; HIGH-AFFINITY ; TOXINS ; CHARYBDOTOXIN ; PROGRAM ; NMR |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000221802000006 |
| 出版者 | WILEY-LISS |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/274075]  |
| 专题 | 新药研究国家重点实验室 中科院受体结构与功能重点实验室 |
| 通讯作者 | Wu, HM |
| 作者单位 | 1.Chinese Acad Sci, Shanghai Inst Organ Chem, State Key Lab Bioorgan & Nat Prod Chem, Shanghai 200032, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Biol Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zhang, NX,Li, MH,Chen, X,et al. Solution structure of BmKK2, a new potassium channel blocker from the venom of Chinese scorpion Buthus martensi Karsch[J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,2004,55(4):835-845. |
| APA | Zhang, NX.,Li, MH.,Chen, X.,Wang, Y.,Wu, G.,...&Wu, HM.(2004).Solution structure of BmKK2, a new potassium channel blocker from the venom of Chinese scorpion Buthus martensi Karsch.PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS,55(4),835-845. |
| MLA | Zhang, NX,et al."Solution structure of BmKK2, a new potassium channel blocker from the venom of Chinese scorpion Buthus martensi Karsch".PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS 55.4(2004):835-845. |
入库方式： OAI收割
来源：上海药物研究所
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