Promiscuous and allele-specific anchors in HLA-DR-binding peptides
| Autor: | David Robert Bolin, Paola Valsasnini, Bela Takacs, Juergen Hammer, Jacqueline Higelin, Francesco Sinigaglia, Khaled A. Tolba |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Genetics
chemistry.chemical_classification MHC class II Binding Sites biology Sequence analysis Molecular Sequence Data Sequence alignment Peptide Peptide binding HLA-DR Antigens Major histocompatibility complex General Biochemistry Genetics and Molecular Biology chemistry HLA-DR biology.protein Humans Amino Acid Sequence Peptides Peptide sequence Sequence Alignment Alleles Bacteriophage M13 |
| Zdroj: | Cell. 74(1) |
| ISSN: | 0092-8674 |
| Popis: | The major histocompatibility complex (MHC) class II molecules are highly polymorphic membrane glycoproteins that bind peptide fragments of proteins and display them for recognition by CD4+ T cells. To understand the effect of human MHC class II polymorphism on peptide-MHC interaction, we have isolated M13 phage from a large M13 peptide display library by selection with DRB1*0401 and DRB1*1101 molecules, as recently described for DRB1*0101. Sequence analysis of the peptide-encoding region of DR-bound phage led to the identification of position-specific anchor residues, defining motifs for peptide binding to DR molecules. The three DR motifs share two anchor residues at relative positions 1 and 4, while allele-specific anchor residues have been identified at position 6. These results provide a biophysical basis for both the promiscuity and the specificity of peptide recognition by DR molecules. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|