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Abstract

An analog of omega-conotoxin MVIIC (Y13A-MVIIC) was synthesized by replacing Tyr13 with Ala to study the role of Tyr13 residue conserved in many omega-conotoxins. Y13A-MVIIC has an overall conformation similar to that of the native toxin, but an enormously reduced ability to displace 125I-omega-conotoxin MVIIC binding to rat cerebellar P2 membranes. These results suggest that Tyr13 is essential for the activity of omega-conotoxins at P/Q-type calcium channels.

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PubMed ID:: 7677735

ScienceOpen disciplines: Chemistry

Keywords: Amino Acid Sequence,Animals,Binding Sites,Binding, Competitive,Calcium Channel Blockers,chemistry,metabolism,Calcium Channels,Cell Membrane,Cerebellum,Conserved Sequence,Disulfides,analysis,Kinetics,Molecular Sequence Data,Peptides,chemical synthesis,pharmacology,Protein Conformation,Purkinje Cells,Rats,Sequence Homology, Amino Acid,Tyrosine,omega-Conotoxins

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ScienceOpen disciplines: Chemistry

Tyr13 is essential for the binding of omega-conotoxin MVIIC to the P/Q-type calcium channel.

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