Solution structure of ω‐conotoxin MVIIA using 2D NMR spectroscopy

FEBS Letters

Nadasdi, Laszlo²  Miljanich, George P.²  Ramachandran, J.²  Basus, Vladimir J.¹ 

[1] Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA;Neurex Corporation, Menlo Park, CA 94025, USA

关键词: Neurotoxin;    Calcium channel blocker;    NMR structure;    Complete relaxation matrix;    Conus magus;   

DOI  :  10.1016/0014-5793(95)00819-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The solution structure of ω-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 β-sheet involving residues 6–8, 20–21, and 24–25. The structure of this toxin is very similar to that of ω-conotoxin GVIA with which is has only 40% sequence homology, but very similar calcium channel binding affinity and selectivity.

【 授权许可】

Unknown