Your browser doesn't support javascript.
loading
pH-dependent intramolecular binding and structure involving Cx43 cytoplasmic domains.
Duffy, Heather S; Sorgen, Paul L; Girvin, Mark E; O'Donnell, Phyllis; Coombs, Wanda; Taffet, Steven M; Delmar, Mario; Spray, David C.
Afiliación
  • Duffy HS; Department of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
J Biol Chem ; 277(39): 36706-14, 2002 Sep 27.
Article en En | MEDLINE | ID: mdl-12151412
pH-induced closure of connexin43 (Cx43) channels involves interaction of the Cx43 carboxyl-terminal (Cx43CT) with a separate "receptor" domain. The receptor location and structure and whether the interaction is directly intramolecular are unknown. Here we show resonant mirror technology, enzyme-linked sorbent assays, and nuclear magnetic resonance (NMR) experiments demonstrating pH-dependent binding of Cx43CT to region 119-144 of Cx43 (Cx43L2), which we propose is the receptor. NMR showed that acidification induced alpha-helical order in Cx43L2, whereas only a minor modification in Cx43CT structure was detected. These data provide the first demonstration of chemically induced structural order and binding between cytoplasmic connexin domains.
Asunto(s)
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conexina 43 Límite: Animals Idioma: En Revista: J Biol Chem Año: 2002 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Buscar en Google
Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Conexina 43 Límite: Animals Idioma: En Revista: J Biol Chem Año: 2002 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos