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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sato K,Raymond C,Martin-Moutot N,Sasaki T,Ohtake A,Minami K,Van Renterghem C,Kim JI,Takahashi M,Seagar MJ

doi

10.1016/s0014-5793(00)01263-1

keywords:

subject

Has Abstract

pub_date

2000-03-10 00:00:00

pages

147-50

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(00)01263-1

journal_volume

469

pub_type

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