Basus V J, Nadasdi L, Ramachandran J, Miljanich G P
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143, USA.
FEBS Lett. 1995 Aug 21;370(3):163-9. doi: 10.1016/0014-5793(95)00819-u.
The solution structure of omega-conotoxin MVIIA (SNX-111), a peptide toxin from the fish hunting cone snail Conus magus and a high-affinity blocker of N-type calcium channels, was determined by 2D NMR spectroscopy. The backbones of the best 44 structures match with an average pairwise RMSD of 0.59 angstroms. The structures contain a short segment of triple-stranded beta-sheet involving residues 6-8, 20-21, and 24-25. The structure of this toxin is very similar to that of omega-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.
芋螺毒素MVIIA（SNX-111）是一种来自以鱼为食的芋螺属的肽毒素，也是N型钙通道的高亲和力阻断剂，其溶液结构通过二维核磁共振光谱法测定。44个最佳结构的主链匹配，平均成对均方根偏差为0.59埃。这些结构包含一段短的三链β-折叠，涉及6-8、20-21和24-25位残基。这种毒素的结构与芋螺毒素GVIA非常相似，它们只有40%的序列同源性，但钙通道结合亲和力和选择性非常相似。
