1MVJ

N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA NMR, 15 STRUCTURES

1MVJ の概要

• エントリーDOI: 10.2210/pdb1mvj/pdb
• 分子名称: SVIB (1 entity in total)
• 機能のキーワード: conus striatus peptide specific to p/q-type voltage sensitive calcium channel, neurotoxin
• 由来する生物種: Conus striatus (striated cone)
• 細胞内の位置: Secreted : P28881
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2750.23

構造登録者

Nielsen, K.J.,Thomas, L.,Lewis, R.J.,Alewood, P.F.,Craik, D.J. (登録日: 1996-08-02, 公開日: 1997-08-12, 最終更新日: 2024-11-20)

主引用文献

Nielsen, K.J.,Thomas, L.,Lewis, R.J.,Alewood, P.F.,Craik, D.J.
A consensus structure for omega-conotoxins with different selectivities for voltage-sensitive calcium channel subtypes: comparison of MVIIA, SVIB and SNX-202.
J.Mol.Biol., 263:297-310, 1996

PubMed Abstract: The omega-conotoxins are a set of structurally related peptides that have a wide range of specificities for different subtypes of the voltage-sensitive calcium channel (VSCC). To understand their VSCC subtype differentiation we studied the structure of two naturally occurring omega-conotoxins, MVIIA (specific to N-type) and SVIB (specific to P/Q-type) and a synthetic hybrid, SNX-202, which has altered specificities to both VSCC subtypes. The secondary structures of the three peptides are almost identical, consisting of a triple-stranded beta-sheet and several turns. A comparison of NMR data emphasizes the structural similarities between the peptides and highlights some minor structural differences. In the three-dimensional structures of SVIB and MVIIA these are manifested as orientational differences between two key loops. The structural rigidity of MVIIA was also examined. H alpha shifts are similar in a range of solvents, indicating that there are no solvent-induced changes in structure. The omega-conotoxins form a consensus structure despite differences in sequence and VSCC subtype specificity. This indicates that the omega-conotoxin macrosites for the N/P/Q-subfamily of VSCCs are related, with specificity for receptor targets being conferred by the positions of functional side-chains on the surface of the peptides.

PubMed: 8913308
DOI: 10.1006/jmbi.1996.0576

実験手法

SOLUTION NMR