Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange - Archive ouverte HAL Access content directly
Journal Articles Biochemistry Year : 2000

Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange

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.

Dates and versions

hal-04119895 , version 1 (06-06-2023)

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R. Andrew Atkinson, Bruno Kieffer, Annick Dejaegere, Finton Sirockin, Jean-François Lefèvre. Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange. Biochemistry, 2000, 39 (14), pp.3908-3919. ⟨10.1021/bi992651h⟩. ⟨hal-04119895⟩
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