Solution structure of the calcium channel antagonist omega-conotoxin GVIA.
Solution structure of the calcium channel antagonist omega-conotoxin GVIA.
复制标题
钙通道拮抗剂 omega-芋螺毒素 GVIA 的溶液结构。
DOI：
10.1002/pro.5560021005
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发表时间：
1993
期刊：
影响因子：
--
通讯作者：
Pardi,A
中科院分区：
文献类型：
--
作者：
Skalicky,JJ;Metzler,WJ;Ciesla,DJ;Galdes,A;Pardi,A
报道了ω-芋螺毒素GVIA的三维溶液结构，GVIA是脊椎动物神经肌肉接头中一种有效的突触前钙通道抑制剂。结构由混合距离几何和约束分子动力学方法生成，该方法使用质子间距离、扭角和氢键约束，来自1H核磁共振数据。低约束违反的GVIA构象会聚为一个共同的多肽折叠。该肽的二级结构是一个反平行的三链β-折叠，含有一个β-发夹和三个紧密的转弯。核磁共振数据与多肽从S9残基到C16残基的区域是一致的，比其余的多肽更具活力。该肽具有两亲性结构，具有带正电荷的亲水侧和包含小疏水区域的相反侧。被认为在结合和功能上重要的残基位于多肽的亲水表面。
The three‐dimensional solution structure is reported for ω‐conotoxin GVIA, which is a potent inhibitor of presynaptic calcium channels in vertebrate neuromuscular junctions. Structures were generated by a hybrid distance geometry and restrained molecular dynamics approach using interproton distance, torsion angle, and hydrogen‐bonding constraints derived from1H NMR data. Conformations of GVIA with low constraint violations converged to a common peptide fold. The secondary structure in the peptide is an antiparallel triple‐stranded β‐sheet containing a β‐hairpin and three tight turns. The NMR data are consistent with the region of the peptide from residues S9 to C16 being more dynamic than the rest of the peptide. The peptide has an amphiphilic structure with a positively charged hydrophilic side and an opposite side that contains a small hydrophobic region. Residues that are thought to be important in binding and function are located on the hydrophilic face of the peptide.