Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.
Virology
; 180(2): 617-24, 1991 Feb.
Article
em En
| MEDLINE
| ID: mdl-1989386
ABSTRACT
The evidence presented shows that the M2 protein of influenza A viruses exists in infected cells as a homotetramer composed of two disulfide-linked dimers held together by noncovalent interactions. The amphiphilic nature of the transmembrane alpha-helical domain is consistent with the protein forming a transmembrane channel with which amantadine, the specific anti-influenza A drug, interacts. Together these features provide a structural basis for the hypothesis that M2 has a proton translocation function capable of regulating the pH of vesicles of the trans-Golgi network, a role important in promoting the correct maturation of the hemagglutinin glycoprotein.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Vírus da Influenza A
/
Proteínas da Matriz Viral
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
Virology
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Reino Unido