菲律宾海蛇毒液中神经毒素a的三维结构。
Three-dimensional structure of neurotoxin a from venom of the Philippines sea snake.
作者信息
Tsernoglou D, Petsko G A
出版信息
Proc Natl Acad Sci U S A. 1977 Mar;74(3):971-4. doi: 10.1073/pnas.74.3.971.
Abstract
The crystal structure of neurotoxin a from the venom of Philippines sea snake Laticauda semifasciata has been determined at 2.5 A resolution by x-ray diffraction. Comparison with the structure of neurotoxin b from the same source indicates that the two toxins differ only by substitution at His 26. Earlier chemical work had suggested a difference in chain length and considerable differences in amino acid composition. The difference between our a and b toxins is the same as that reported from sequence analysis for the related erabutoxins a and b from Japanese sea snake, and suggests that the Philippines toxin may be identical to erabutoxin. The replacement of His 26 by a shorter side-chain in toxin a has no effect on the structure of the rest of the molecule. In particular, the protruding loop, which we believe interacts with the acetylcholine receptor, is not affected, even though His 26 is in the loop.
摘要
通过X射线衍射，已在2.5埃分辨率下测定了菲律宾海蛇半环扁尾海蛇毒液中神经毒素a的晶体结构。与来自同一来源的神经毒素b的结构比较表明，这两种毒素仅在组氨酸26处的取代有所不同。早期的化学研究表明链长存在差异且氨基酸组成有显著差异。我们的毒素a和b之间的差异与日本海蛇相关的 erabutoxins a和b的序列分析报告的差异相同，这表明菲律宾毒素可能与 erabutoxin相同。毒素a中组氨酸26被较短侧链取代对分子其余部分的结构没有影响。特别是，我们认为与乙酰胆碱受体相互作用的突出环不受影响，尽管组氨酸26在该环中。
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