Structural diversity of human class II histocompatibility molecules induced by peptide ligands

FEBS Letters

Georges, Bertrand²  Loing, Estelle¹  Gras-Masse, Helene¹  Auriault, Claude²  Melnyk, Oleg¹  Neveu, Raphaële² 

[1] Laboratoire de Chimie des Biomolécules CNRS UMR 8525, Lille, France;Laboratoire d'Immunopathologie Cellulaire des Maladies Infectieuses, CNRS UMR 8527, Lille, France

关键词: Soluble MHC class II;    DRB1*0101;    Stability;    Conformation;    Peptide binding;    PFR;    peptide flanking residue;    MHC;    major histocompatibility complex;   

DOI  :  10.1016/S0014-5793(00)01981-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

SDS–PAGE analyses of stable HLA-DR1 complexes indicate that the binding of T cell epitopes can lead to multiple conformational variants. Whereas short T epitopes (<14-mer) induce complexes with apparent MW ranging from 47 to 57 kDa, longer peptides form generally high mobility complexes (44–45 kDa). The generation of HLA-DR1 conformational variants appears dependent on core peptide residues fitting inside the groove but can additionally be attributed to the presence of N- and C-terminal flanking residues (PFRs) acting as a complementary mechanism. These PFRs can jointly affect major histocompatibility complex class II conformation and stability, supporting the existence of alternative contacts at a distance from the classical binding site.

【 授权许可】

Unknown