We are analyzing https://link.springer.com/article/10.1007/bf02602781.

Title:
Analysis of anchor residues in a naturally processed HLA-DR53 ligand | Immunogenetics
Description:
Immunogenetics - The peptide motif of the HLA-DR53 (DRB4*0101) molecule, which is associated with autoimmune diseases including Vogt-Koyanagi-Harada
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article, hladr, google, scholar, pubmed, peptides, cas, peptide, binding, molecules, naturally, motif, processed, class, immunol, position, residue, access, mhc, privacy, cookies, content, analysis, katagiri, bound, information, publish, search, kobayashi, kimura, molecule, assay, human, antigen, related, data, log, journal, research, immunogenetics, residues, kokubo, abe, sato, hladrdr, cell, positively, hydrophobic, motifs, endogeneous,

Topics {✒️}

hla-class ii-molecules hla-dr53-specific binding motif single-alanine-substituted nonbiotinylated peptides naturally processed hla-dr9/dr53 month download article/chapter peptide-binding assay based hla-dr β chain hla-dr1 binding peptides purified hla-dr molecules mhc proteins naturally occurring hla-dr53 hla-dr-binding peptides hla-dr9/dr53 molecules b-cell alloantigenic determinant hla-dq-restricted cd4+ peptide binding assay hla-dr molecules hla-dr antigen inhibitory motif hla-dr53 molecules vogt-koyanagi-harada' hla-dr allele naturally processed peptides hla-dr9/dr53 hla-dr53 molecule full article pdf hla-drβ chain treptococcal m12 protein privacy choices/manage cookies cell epitope restricted hla-dr53 moleule plastin p581–595 peptide influenza virus peptide related subjects article immunogenetics aims hla class peptide motif allele-specific anchors streptococcal antigen present hydrophobic residue peptide binding positively charged residue check access mhc ligands instant access endogeneous peptides bound european economic area m13 display library amino acid positions m13 display libraries

Schema {🗺️}

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         headline:Analysis of anchor residues in a naturally processed HLA-DR53 ligand
         description:The peptide motif of the HLA-DR53 (DRB4*0101) molecule, which is associated with autoimmune diseases including Vogt-Koyanagi-Harada's syndrome, was determined by peptide binding assay using human L plastin p581–595 peptide and its substituted analogues. L plastin p581–595 peptide is one of the naturally processed peptides bound to HLA-DR9/DR53 (DRB1*0901/DRB4*0101) molecules. The binding affinity of each peptide to the HLA-DR53 molecule was measured by fluorescence intensity of biotinylate peptides to L cell transfectants expressing HLA-DR53 molecules, followed by treatment with avidin-fluorescence. Binding of biotinylated peptides to HLA-DR53 molecules was not inhibited by all single-alanine-substituted nonbiotinylated peptides, indicating that the replaced position was important for binding to the HLA-DR53 moleule. The inhibitory motif is considered to be an HLA-DR53-specific binding motif, composed of a positively charged residue (K) at position 1, a hydrophobic residue (I) at position 4, positively charged residue (R or K) at position 8 or 9, and another hydrophobic residue (I) at position 10. This predicted motif is different from the binding motifs of other HLA-DR molecules. binding peptides in combination with functional analyses, by alignment of sequenced endogeneous peptides, and by the use of an M13 display library (Rammensee et al. 1995; Hammer et al. 1993, 1992). No sequence information has been reported for naturally occurring HLA-DR53 (DRB4*0101)-associated peptides partly because their expression on the cell surface is relatively low for sequencing endogeneous self-peptides (Kinouchi et al. 1995). It has been shown that HLA-DR53 is positively associated with Vogt-Koyanagi-Harada's Syndrome in Japanese subjects (Moriuchi et al. 1979). The identification of a peptide motif for HLA-DR53 may help in understanding the mechanisms of this disease. We have previously reported that naturally processed peptides bound to HLA-DR9/DR53 molecules (Futaki et al. 1995). In this report, we determined the peptide which could bind to the HLA-DR53 molecule and we identified a putative HLA-DR53-specific binding motif by a peptide binding assay using L-cell transfectants expressing HLA-DR molecules.
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      headline:Analysis of anchor residues in a naturally processed HLA-DR53 ligand
      description:The peptide motif of the HLA-DR53 (DRB4*0101) molecule, which is associated with autoimmune diseases including Vogt-Koyanagi-Harada's syndrome, was determined by peptide binding assay using human L plastin p581–595 peptide and its substituted analogues. L plastin p581–595 peptide is one of the naturally processed peptides bound to HLA-DR9/DR53 (DRB1*0901/DRB4*0101) molecules. The binding affinity of each peptide to the HLA-DR53 molecule was measured by fluorescence intensity of biotinylate peptides to L cell transfectants expressing HLA-DR53 molecules, followed by treatment with avidin-fluorescence. Binding of biotinylated peptides to HLA-DR53 molecules was not inhibited by all single-alanine-substituted nonbiotinylated peptides, indicating that the replaced position was important for binding to the HLA-DR53 moleule. The inhibitory motif is considered to be an HLA-DR53-specific binding motif, composed of a positively charged residue (K) at position 1, a hydrophobic residue (I) at position 4, positively charged residue (R or K) at position 8 or 9, and another hydrophobic residue (I) at position 10. This predicted motif is different from the binding motifs of other HLA-DR molecules. binding peptides in combination with functional analyses, by alignment of sequenced endogeneous peptides, and by the use of an M13 display library (Rammensee et al. 1995; Hammer et al. 1993, 1992). No sequence information has been reported for naturally occurring HLA-DR53 (DRB4*0101)-associated peptides partly because their expression on the cell surface is relatively low for sequencing endogeneous self-peptides (Kinouchi et al. 1995). It has been shown that HLA-DR53 is positively associated with Vogt-Koyanagi-Harada's Syndrome in Japanese subjects (Moriuchi et al. 1979). The identification of a peptide motif for HLA-DR53 may help in understanding the mechanisms of this disease. We have previously reported that naturally processed peptides bound to HLA-DR9/DR53 molecules (Futaki et al. 1995). In this report, we determined the peptide which could bind to the HLA-DR53 molecule and we identified a putative HLA-DR53-specific binding motif by a peptide binding assay using L-cell transfectants expressing HLA-DR molecules.
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      dateModified:
      pageStart:366
      pageEnd:371
      sameAs:https://doi.org/10.1007/BF02602781
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         Peptide
         Major Histocompatibility Complex
         Binding Motif
         Hydrophobic Residue
         Inhibitory Motif
         Immunology
         Human Genetics
         Gene Function
         Cell Biology
         Allergology
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