生物
肽
主要组织相容性复合体
噬菌体展示
肽库
糖蛋白
遗传学
肽序列
人类白细胞抗原
分子生物学
计算生物学
生物化学
基因
抗原
作者
Juergen Hammer,Paola Valsasnini,Khaled A. Tolba,David Bolin,Jacqueline Higelin,B. Takács,Francesco Sinigaglia
出处
期刊:Cell
[Elsevier]
日期:1993-07-01
卷期号:74 (1): 197-203
被引量:370
标识
DOI:10.1016/0092-8674(93)90306-b
摘要
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.
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