[HTML][HTML] Main chain hydrogen bond interactions in the binding of proline-rich gluten peptides to the celiac disease-associated HLA-DQ2 molecule
Binding of peptide epitopes to major histocompatibility complex proteins involves multiple
hydrogen bond interactions between the peptide main chain and major histocompatibility
complex residues. The crystal structure of HLA-DQ2 complexed with the αI-gliadin epitope
(LQPFPQPELPY) revealed four hydrogen bonds between DQ2 and peptide main chain
amides. This is remarkable, given that four of the nine core residues in this peptide are
proline residues that cannot engage in amide hydrogen bonding. Preserving main chain …
hydrogen bond interactions between the peptide main chain and major histocompatibility
complex residues. The crystal structure of HLA-DQ2 complexed with the αI-gliadin epitope
(LQPFPQPELPY) revealed four hydrogen bonds between DQ2 and peptide main chain
amides. This is remarkable, given that four of the nine core residues in this peptide are
proline residues that cannot engage in amide hydrogen bonding. Preserving main chain …