Convergent recognition of the IgE binding site on the high-affinity IgE receptor.
Structure
; 12(7): 1289-301, 2004 Jul.
Article
em En
| MEDLINE
| ID: mdl-15242605
ABSTRACT
Two structurally distinct classes of peptides were recently identified by phage display that bind the high-affinity IgE receptor, FcepsilonRI, and block IgE binding and subsequent receptor activation. Both classes adopt highly stable structures in solution, one forming a beta hairpin, with the other forming a helical "zeta" structure. Despite these differences, the two classes bind competitively to the same site on the receptor. Structural analyses of both peptide-receptor complexes by NMR spectroscopy and/or X-ray crystallography reveal that the unrelated peptide scaffolds have nevertheless converged to present a similar three-dimensional surface to interact with FcepsilonRI and that their modes of interaction share a key feature of the IgE-FcepsilonRI complex, the proline/tryptophan sandwich.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Ligação Competitiva
/
Imunoglobulina E
/
Receptores de IgE
Limite:
Humans
Idioma:
En
Revista:
Structure
Ano de publicação:
2004
Tipo de documento:
Article