| 摘要: |
| 海葵神经毒素是一类能与可激动细胞电压门控钠通道发生亲和作用的海洋多肽毒素。根据80–90年代中期国际上对海葵神经毒素的研究成果，重点对其结构特征、结构与功能的关系进行综合评述。已有的结果表明，所有已发现的海葵神经毒素其同源性较高，拥有相似的二级结构和三维结构；不规则环状结构的正确构象对毒素的心肌刺激活性是至关重要的。通过比较研究方法，作者认为：typeⅠ毒素的残基18和typeⅡ毒素的残基17侧链具有强流水性，对毒素的活性起关键作用；而typeⅠ毒素残基43和typeⅡ毒素残基40的疏水烷基侧链，可能对海葵毒素的形成起决定作用。 |
| 关键词: 海葵多肽毒素 结构 功能 |
| DOI： |
| 分类号: |
| 基金项目:“九五”国家科技攻关项目，96C010504号 |
附件 |
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| RECENT ADVANCES IN STRUCTURE AND FUNCTION OF SEA ANEMONE POLYPEPTIDE NEUROTOXINS |
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ZHANG Jun-shun,ZHANG Pei-jun
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Insititule of Oceanology, The Chinese Academy of deiences, Qingdao, 266071
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| Abstract: |
| Sea anemone neurotoxins are a series of marine polypeptide toxins which possess binding affinity for voltage-gated sodium channels of excitable cells. In accordance studies in the 1980’s and 1990’s on the structure and function of anemone neurotoxins, the first, secondary and tertiary structure of anemone neurotoxins, and the relationship between structure and function are summarized. It is concluded that the anemone polypeptides so far identified are homologous and the main secondary and tertiary structure features of theirs are very similar, correct conformation of the irregular loop of anemone neurotoxins is critical for cardiostimulant activity. The result of a comparative study demonstrates that the strongly hydrophobic residues at position 18 and 17 in Types I and II neurotoxins, respectively, play a critical role in high affinity channel binding, while hydrophobic residues Ile-43 and Ile-40 in both Types I and II neurotoxins are probably an important structural determinant the Ap-A and Ap-B residues at positions 12 and 49 are essential for both high affinity and isoform discrimination. Consequently, these characteristics are essential for the application of the anemone toxin to the design of new cardiotonic drugs. |
| Key words: Anemone, polypeptides, Structure, Function |
