PEPTIDES PRESENTED TO THE IMMUNE-SYSTEM BY THE MURINE CLASS-II MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE-I-A(D)
PEPTIDES PRESENTED TO THE IMMUNE-SYSTEM BY THE MURINE CLASS-II MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULE-I-A(D)
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DOI：
10.1126/science.1319610
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发表时间：
1992-06-26
期刊：
影响因子：
56.9
通讯作者：
SETTE, A
中科院分区：
文献类型：
--
作者：
HUNT, DF;MICHEL, H;SETTE, A
650至2000种不同的肽与主要组织相容性复合体II类分子I-A（d）相关。其中9个序列是通过自动Edman降解和串联质谱法的组合获得的。所有的肽都来源于抗原呈递细胞自身合成的分泌性或整合性膜蛋白。肽的长度为16至18个残基，具有参差不齐的NH 2-和COOH-末端，并且含有六个残基的结合基序，该基序在肽链内被交替放置。截短肽的结合数据表明，II类分子上的肽结合沟可以在两端开放。
Between 650 and 2000 different peptides are associated with the major histocompatibility complex class II molecule I-A(d). Sequences for nine of these were obtained by a combination of automated Edman degradation and tandem mass spectrometry. All of the peptides are derived from secretory or integral membrane proteins that are synthesized by the antigen-presenting cell itself. Peptides were 16 to 18 residues long, had ragged NH2- and COOH-termini, and contained a six-residue binding motif that was variably placed within the peptide chain. Binding data on truncated peptides suggest that the peptide binding groove on class II molecules can be open at both ends.