Unusual binding mode of scorpion toxin BmKTX onto potassium channels relies on its distribution of acidic residues.
Biochem Biophys Res Commun
; 447(1): 70-6, 2014 Apr 25.
Article
em En
| MEDLINE
| ID: mdl-24704423
ABSTRACT
Besides classical scorpion toxin-potassium channel binding modes, novel modes remain unknown. Here, we report a novel binding mode of native toxin BmKTX towards Kv1.3 channel. The combined experimental and computational data indicated that BmKTX-D33H analog used the classical anti-parallel ß-sheet domain as the channel-interacting interface together with the conserved channel pore-blocking Lys(26). However, the wild-type BmKTX was found to use Arg(23) rather than Lys(26) as the new pore-blocking residue, and mainly adopt the turn motif between the α-helix and antiparallel ß-sheet domains to recognize Kv1.3 channel. Together, these findings not only reveal that scorpion toxin-potassium channel interaction modes are more diverse than thought, but also highlight the functional role of toxin acidic residues in mediating diverse toxin-potassium channel binding modes.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Venenos de Escorpião
/
Canal de Potássio Kv1.3
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article