Torres Allan M, Bansal Paramjit, Alewood Paul F, Bursill Jane A, Kuchel Philip W, Vandenberg Jamie I
School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
FEBS Lett. 2003 Mar 27;539(1-3):138-42. doi: 10.1016/s0014-5793(03)00216-3.
The three-dimensional structure of chemically synthesized CnErg1 (Ergtoxin), which specifically blocks HERG (human ether-a-go-go-related gene) K+ channels, was determined by nuclear magnetic resonance spectroscopy. CnErg1 consists of a triple-stranded beta-sheet and an alpha-helix, as is typical of K+ channel scorpion toxins. The peptide structure differs from the canonical structures in that the first beta-strand is shorter and is nearer to the second beta-strand rather than to the third beta-strand on the C-terminus. There is also a large hydrophobic patch on the surface of the toxin, surrounding a central lysine residue, Lys13. We postulate that this hydrophobic patch is likely to form part of the binding surface of the toxin.
通过核磁共振光谱法确定了化学合成的CnErg1（Erg毒素）的三维结构，该毒素特异性阻断人类ether-a-go-go相关基因（HERG）钾通道。CnErg1由三股β折叠和一个α螺旋组成，这是钾通道蝎毒素的典型结构。该肽结构与经典结构的不同之处在于，第一条β链较短，且在C端更靠近第二条β链而非第三条β链。毒素表面还有一个大的疏水区域，围绕着一个中心赖氨酸残基Lys13。我们推测这个疏水区域可能构成毒素结合表面的一部分。
