The peptide-binding motif of HLA-B*3505
β Scribed by Amanda Kenneally; Bin Liang; Linda D. Barber
- Publisher
- Springer-Verlag
- Year
- 2000
- Tongue
- English
- Weight
- 58 KB
- Volume
- 51
- Category
- Article
- ISSN
- 0093-7711
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π SIMILAR VOLUMES
HLA-B\*3501 and HLA-B\*3503 molecules differ by a single amino acid located in the [~-pleated sheet of the c~2 domain. In order to clarify the basis of the strict distinction between these highly related class I molecules by several alloreactive T cell clones , we determined the motif of HLA-B\*3503
Eight nonamer peptides that comply with the major anchor residue motifs (the combination of amino acid residues at positions 2 and 9), R - K and R - R, of HLA-B27 (B\*2705)-binding peptides were synthesized and tested for their direct binding to HLA class I alpha chains by the HLA class I alpha chai