24
views
0
recommends
+1 Recommend
0 collections
    0
    shares
      • Record: found
      • Abstract: not found
      • Article: not found

      MHC ligands and peptide motifs: first listing

      , ,
      Immunogenetics
      Springer Nature

      Read this article at

      ScienceOpenPublisherPubMed
      Bookmark
          There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.

          Related collections

          Most cited references102

          • Record: found
          • Abstract: found
          • Article: not found

          Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.

          The three-dimensional structure of the class II histocompatibility glycoprotein HLA-DR1 from human B-cell membranes has been determined by X-ray crystallography and is similar to that of class I HLA. Peptides are bound in an extended conformation that projects from both ends of an 'open-ended' antigen-binding groove. A prominent non-polar pocket into which an 'anchoring' peptide side chain fits is near one end of the binding groove. A dimer of the class II alpha beta heterodimers is seen in the crystal forms of HLA-DR1, suggesting class II HLA dimerization as a mechanism for initiating the cytoplasmic signalling events in T-cell activation.
            Bookmark
            • Record: found
            • Abstract: found
            • Article: not found

            Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.

            An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.
              Bookmark
              • Record: found
              • Abstract: not found
              • Article: not found

              The shared epitope hypothesis. an approach to understanding the molecular genetics of susceptibility to rheumatoid arthritis

                Bookmark

                Author and article information

                Journal
                Immunogenetics
                Immunogenetics
                Springer Nature
                0093-7711
                1432-1211
                February 1995
                February 1995
                : 41
                : 4
                : 178-228
                Article
                10.1007/BF00172063
                7890324
                2bdb90aa-4e8d-4fd7-81bf-855b22f6cc53
                © 1995
                History

                Comments

                Comment on this article