1DW4

NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: CONSTRAINTS ON DISULPHIDE BRIDGES

1DW4 の概要

• エントリーDOI: 10.2210/pdb1dw4/pdb
• 関連するPDBエントリー: 1DW5
• 分子名称: OMEGA-CONOTOXIN MVIIA (1 entity in total)
• 機能のキーワード: conotoxin, calcium channel, conformational exchange, toxin
• 細胞内の位置: Secreted: P05484
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2650.22

構造登録者

Atkinson, R.A.,Kieffer, B.,Dejaegere, A.,Sirockin, F.,Lefevre, J.-F. (登録日: 2000-01-24, 公開日: 2000-03-01, 最終更新日: 2024-11-20)

主引用文献

Atkinson, R.A.,Kieffer, B.,Dejaegere, A.,Sirockin, F.,Lefevre, J.F.
Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange.
Biochemistry, 39:3908-3919, 2000

PubMed Abstract: omega-Conotoxin MVIIA is a 25-residue, disulfide-bridged polypeptide from the venom of the sea snail Conus magus that binds to neuronal N-type calcium channels. It forms a compact folded structure, presenting a loop between Cys8 and Cys15 that contains a set of residues critical for its binding. The loop does not have a unique defined structure, nor is it intrinsically flexible. Broadening of a subset of resonances in the NMR spectrum at low temperature, anomalous temperature dependence of the chemical shifts of some resonances, and exchange contributions to J(0) from (13)C relaxation measurements reveal that conformational exchange affects the residues in this loop. The effects of this exchange on the calculated structure of omega-conotoxin MVIIA are discussed. The exchange appears to be associated with a change in the conformation of the disulfide bridge Cys8-Cys20. The implications for the use of the omega-conotoxins as a scaffold for carrying other functions is discussed.

PubMed: 10747778
DOI: 10.1021/bi992651h

実験手法

SOLUTION NMR