Three-dimensional structure of the mini-M conotoxin mr3a.
Three-dimensional structure of the mini-M conotoxin mr3a.
复制标题
mini-M 芋螺毒素 mr3a 的三维结构。
DOI:
10.1021/bi0353732
复制
发表时间:
2004
期刊:
影响因子:
2.9
通讯作者:
Poulter,CDale
中科院分区:
文献类型:
--
作者:
McDougal,OwenM;Poulter,CDale
Conotoxin mr3a from the venom ofConus marmoreus, a novel peptide that induces rolling seizures in mice, has the peptide sequence GCCGSFACRFGCVOCCV, where O istrans-4-hydroxyproline, and the chain is cross-linked with disulfide bonds between Cys-2 and Cys-16, Cys-3 and Cys-12, and Cys-8 and Cys-15. The tertiary structure of mr3a was determined by 2D1H NMR in combination with a standard distance−geometry algorithm. The final set of 22 structures for the peptide had a mean global backbone RMS deviation of 0.53 ± 0.22 Å based on 51 NOE, 6 hydrogen bond, 6 ϕ dihedral angle, and 3 disulfide bond constraints. Conotoxin mr3a is the first example of the new mini-M branch of conopeptides in the M superfamily. Members of the maxi-M branch, whose structures are known, include the μ- and ψ-conotoxins, both of which share a common disulfide bond connectivity. Although mr3a has the same arrangement of Cys residues as the μ- and ψ-conotoxins, its disulfide connectivity is different. This gives mr3a a distinctive “triple-turn” backbone.