Selected article for: "binding affinity and class ii"

Author: A.J.W. Haasnoot; M.W. Schilham; S.S.M. Kamphuis; P.C.E. Hissink Muller; A. Heiligenhaus; D. Foell; R.A. Ophoff; T.R.D.J. Radstake; A.I. Den Hollander; T.H.C.M. Reinards; S. Hiddingh; N. Schalij-Delfos; E.P.A.H. Hoppenreijs; M.A.J. van Rossum; C. Wouters; R.K. Saurenmann; N. Wulffraat; R. ten Cate; J.H. de Boer; S.L. Pulit; J.J.W. Kuiper
Title: An amino acid motif in HLA-DRß1 distinguishes patients with uveitis in juvenile idiopathic arthritis
  • Document date: 2017_5_22
  • ID: 4it5c9n2_18
    Snippet: Polymorphisms in the beta chain specify the peptide binding preference of the HLA-DR molecule. Serine at position 11, as well as the adjacent associated amino acids at position 10 -13, are located in the bottom of the antigen-binding groove of the HLA-DRB1 protein (Figure 2) , suggesting that different peptide-binding preferences of HLA-DRB1 may confer risk for developing uveitis. To explore if the presence of serine at position 11 affects peptid.....
    Document: Polymorphisms in the beta chain specify the peptide binding preference of the HLA-DR molecule. Serine at position 11, as well as the adjacent associated amino acids at position 10 -13, are located in the bottom of the antigen-binding groove of the HLA-DRB1 protein (Figure 2) , suggesting that different peptide-binding preferences of HLA-DRB1 may confer risk for developing uveitis. To explore if the presence of serine at position 11 affects peptide-MHCII interactions, we compared the predicted binding affinity for 13 common HLA-DRB1 allotypes (representing 79% of DRB1 alleles in cases) using a large panel of >80,000 peptides based on human iris proteome data (Materials and Methods and Supplementary Table 4) using the NetMHCIIpan server. 38 Briefly, the neural networkbased NetMHCIIpan algorithm is capable of reliably detecting differences between peptidebinding repertoires of highly similar MHC class II molecules.

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