Functional consequences of deleting the two C-terminal residues of the scorpion toxin BmTX3.
Biochim Biophys Acta
; 1646(1-2): 152-6, 2003 Mar 21.
Article
em En
| MEDLINE
| ID: mdl-12637022
ABSTRACT
We deleted the two C-terminal residues of the scorpion toxin BmTx3, a peptidyl inhibitor of a transient A-type K(+) current in striatum neurons in culture, to assess their contribution to receptor recognition. The sBmTX3-delYP analog was shown to have a native-like structure in one-dimensional 1H-nuclear magnetic resonance (NMR) spectroscopy. We found that sBmTX3-delYP bound to its receptor less efficiently than the wild-type molecule (by a factor of about 10(5)) in binding assays with rat brain membranes, and that this molecule did not block the A-type K(+) current (at a concentration of 35 microM) in whole-cell patch clamp experiments with striatum neurons. Also, these results show that the A-type K(+) channel blocked by BmTX3 should have a canonical K(+) channel pore structure.
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Base de dados:
MEDLINE
Assunto principal:
Venenos de Escorpião
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
França