Accueil > Publications > Recherche par années > Années 2000 > 2005

Kellenberger, C ; Roussel, A ; Malissen, B

The H-2K(k) MHC peptide-binding groove anchors the backbone of an octameric antigenic peptide in an unprecedented mode

Journal of Immunology 175 (6) 3819-3825

par Administrateur - publié le

Abstract :

A wealth of data has accumulated on the structure of mouse MHC class I (MHCI) molecules encoded by the H-2(h) and H-2(d) haplotypes. In contrast, there is a dearth of structural data regarding H-2(k)-encoded molecules. Therefore, the structures of H-2K(k) complexed to an octameric peptide from influenza A virus (HA(259-266)) and to a nonameric peptide from SV40 (SV40(560-568)) have been determined by x-ray crystallography at 2.5 and 3.0 angstrom resolutions, respectively. The structure of the H-2K(k)-HA(259-266) complex reveals that residues located on the floor of the peptide-binding groove contact directly the backbone of the octameric peptide and force it to lie deep within the H-2K(k) groove.