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May 1, 1994The Journal of ImmunologyOpen Access

Role of the polymorphic residues in HLA-DR molecules in allele-specific binding of peptide ligands.

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Authors

KMK. Wayne MarshallUniversity of Wisconsin–MadisonALAi Feng LiuSouthwest UniversityJCJosé CanalesConsejo Superior de Investigaciones Científicas

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Implication

Analysis of HLA-DR alleles reveals how polymorphic residues affect peptide binding, suggesting functional implications.

Key Points

  • This research examines how specific polymorphic residues in HLA-DR molecules influence their ability to bind peptide ligands.
  • Analyzed peptide binding across different HLA-DR alleles using a set of amino acid positions.
  • Evaluated binding affinity via IC50 values for alleles with specific polymorphisms at positions 57 and 86.
  • Correlated structural features of peptides with polymorphic residues in the binding site to define allele-specific requirements.
  • HLA-DR alleles with glycine at position 86 and aspartic acid at position 57 exhibited lower IC50 values, indicating stronger binding affinity.
  • Peptide binding was influenced by the size of the amino acid at position 86, affecting steric requirements.
  • Most free energy of binding resulted from interactions with the peptide backbone and a hydrophobic amino acid at the third position.

Cite This Study

Marshall et al. (1994) studied this question.

synapsesocial.com/papers/6a1fc4fa4d47af2d82bc3f70https://doi.org/10.4049/jimmunol.152.10.4946
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