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Binding of Ala-scanning analogs of omega-conotoxin MVIIC to N- and P/Q-type calcium channels.

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metabolism, omega-Conotoxins, Alanine, chemistry, Amino Acid Sequence, Animals, Calcium Channel Blockers, chemical synthesis, Calcium Channels, N-Type, Calcium Channels, P-Type, Calcium Channels, Q-Type, Cerebellum, Chromatography, High Pressure Liquid, Circular Dichroism, Disulfides, In Vitro Techniques, Intracellular Membranes, physiology, Ion Channel Gating, Models, Molecular, Molecular Sequence Data, Protein Binding, Rats, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Structure-Activity Relationship

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      Abstract

      omega-Conotoxin MVIIC binds to P/Q-type calcium channels with high affinity and N-type channels with low affinity. To reveal the residues essential for subtype selectivity, we synthesized Ala-scanning analogs of MVIIC. Binding assays using rat cerebellar P(2) membranes suggested that Thr(11), Tyr(13) and Lys(2) are essential for binding to both N- and P/Q-type channels, whereas Lys(4) and Arg(22) are important for binding to P/Q-type channels. These results suggest that MVIIC interacts with P/Q-type channels via a large surface, in good agreement with previous observations using chimeric analogs.

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      10713260

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