Biochim Biophys Acta 2001 Jun 06;15122:329-34. doi: 10.1016/s0005-2736(01)00336-4.

The influence exerted by the beta(3) subunit on MVIIA omega-conotoxin binding to neuronal N-type calcium channels.

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In the present study, two-electrode voltage-clamp techniques have been used to assess the interaction between the MVIIA omega-conotoxin and an isoform of the N-type Ca(2+) channel alpha subunit (alpha(1B-d)). Cloned alpha(1B-d) Ca(2+) channels were expressed in Xenopus laevis oocytes in the presence and absence of the beta(3) subunit. Coexpression of the beta(3) subunit significantly shifted the IC(50) value for MVIIA inhibition of central N-type Ca(2+) channel current. Analysis of the peak conductance vs. depolarising voltage dependence suggested that the beta(3) subunit has no apparent effect on the gating charge which accompanies the closed-open transition of the channels. Instead, coexpression of the beta(3) subunit led to an approx. 10 mV shift to more hyperpolarised potentials in the voltage-dependent activation of N-type Ca(2+) channels. We conclude that MVIIA alters the surface charge on the N-type Ca(2+) channels and might induce allosteric changes on the structure of the channel, leading to an increase in the dissociation constant of MVIIA binding.

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