ERp57 interacts with conserved cysteine residues in the MHC class I peptide-binding groove.
FEBS Lett
; 581(10): 1988-92, 2007 May 15.
Article
em En
| MEDLINE
| ID: mdl-17467700
ABSTRACT
The oxidoreductase ERp57 is a component of the major histocompatibility complex (MHC) class I peptide-loading complex. ERp57 can interact directly with MHC class I molecules, however, little is known about which of the cysteine residues within the MHC class I molecule are relevant to this interaction. MHC class I molecules possess conserved disulfide bonds between cysteines 101-164, and 203-259 in the peptide-binding and alpha3 domain, respectively. By studying a series of mutants of these conserved residues, we demonstrate that ERp57 predominantly associates with cysteine residues in the peptide-binding domain, thus indicating ERp57 has direct access to the peptide-binding groove of MHC class I molecules during assembly.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Antígenos de Histocompatibilidade Classe II
/
Sequência Conservada
/
Isomerases de Dissulfetos de Proteínas
/
Cisteína
Limite:
Animals
/
Humans
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Reino Unido