Peptide motif of the class I molecule HLA-B*1503
โ Scribed by Kiley R. Prilliman; Mark Lindsey; Jihua Wang; Kenneth W. Jackson; W. H. Hildebrand
- Publisher
- Springer-Verlag
- Year
- 1999
- Tongue
- English
- Weight
- 88 KB
- Volume
- 49
- Category
- Article
- ISSN
- 0093-7711
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
MHC molecules are peptide receptors of peculiar specificity (Falk et al. 1991; for review, see Rammensee et al. 1993). Each MHC allelic product has its individual peptide specificity, summarized as a peptide motif that is characterized by the position and occupancy of anchor residues whose side chai
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
gene used for transfection had been cloned from a Japanese individual and was confirmed by sequencing to be B'I501 (M. Takiguchi and co-workers, unpublished results). Transfectants were expanded in about 30 to 50 1 of roller bottle cultures. Cell pellets of 20 to 50 ml were detergent lysed, and the