ANNEE : 1995Tyr13 is essential for the binding of omega-conotoxin MVIIC to the P/Q-type calcium channel. AUTEURS :
Kim JI, Takaashi M, Moutot N
, Seagar M
, Ohtake A, Sato K.REVUE :
Biochem Biophys Res CommunN° Pubmed : 7677735
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.