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Structural diversity of human class II histocompatibility molecules induced by peptide ligands
Author(s) -
Georges Bertrand,
Loing Estelle,
Neveu Raphaële,
Melnyk Oleg,
Gras-Masse Helene,
Auriault Claude
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01981-5
Subject(s) - epitope , peptide , major histocompatibility complex , chemistry , human leukocyte antigen , molecule , biophysics , stereochemistry , biochemistry , biology , antigen , genetics , gene , organic chemistry
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.