Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides.
J Mol Biol
; 312(5): 1059-71, 2001 Oct 05.
Article
em En
| MEDLINE
| ID: mdl-11580250
ABSTRACT
Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Antígenos H-2
/
Vírus da Coriomeningite Linfocítica
/
Antígenos Virais
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article