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Characterization of three functional sites in alpha beta 1 DR of DRw13. All three sites are potentially involved in major histocompatibility complex-peptide interaction.

Abstract
An HLA-DR product encoded by the HLA-DRw13/Dw19 haplotype has been identified as the HLA class II molecule involved in antigen presentation to several influenza-specific helper T cell clones. Three different functional sites were identified on this molecule by comparing the structure of HLA-DR products of known sequences and their ability to efficiently present foreign antigen to the T cell clones. These functional sites were mapped on the recently proposed three-dimensional structure of HLA class II molecules. From their position, these sites are all potentially involved in HLA-peptide interaction and capable of affecting the binding and/or the conformation of the foreign peptide. This suggests that polymorphic residues essential in major histocompatibility complex restriction are mostly involved in peptide binding.
AuthorsG Sterkers, J M Tiercy, D Zeliszewski, J P Levy, B Mach
JournalEuropean journal of immunology (Eur J Immunol) Vol. 19 Issue 9 Pg. 1585-90 (Sep 1989) ISSN: 0014-2980 [Print] Germany
PMID2529124 (Publication Type: Journal Article)
Chemical References
  • Antigens, Viral
  • HLA-DR Antigens
Topics
  • Amino Acid Sequence
  • Antigen-Presenting Cells (immunology)
  • Antigens, Viral (immunology)
  • Clone Cells
  • HLA-DR Antigens (immunology)
  • Haplotypes
  • Humans
  • In Vitro Techniques
  • Influenza A virus (immunology)
  • Molecular Sequence Data
  • Protein Conformation
  • Structure-Activity Relationship
  • T-Lymphocytes, Helper-Inducer (immunology)

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