Structures of an MHC class II molecule with covalently bound single peptides
Structures of an MHC class II molecule with covalently bound single peptides
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DOI：
10.1126/science.272.5264.1001
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发表时间：
1996-05-17
期刊：
影响因子：
56.9
通讯作者：
Kappler, J
中科院分区：
文献类型：
--
作者：
Fremont, DH;Hendrickson, WA;Kappler, J
测定了小鼠主要组织相容性复合体（MHC）II类分子I-E（k）的高分辨率X射线晶体结构，I-E（k）由两种抗原肽中的任一种占据。它们揭示了I-E（k）肽结合基序的结构基础，并提出了其他等位基因的一般原则。预测在所有鼠I-E和人DR MHC II类分子中保守的结合沟中的酸性氨基酸的埋藏簇表明pH如何影响MHC结合或肽的交换。这些结构还补充了关于单个肽残基对T细胞受体识别的重要性的突变研究。
The high-resolution x-ray crystal structures of the murine major histocompatibility complex (MHC) class II molecule, I-E(k), occupied by either of two antigenic peptides were determined. They reveal the structural basis for the I-E(k) peptide binding motif and suggest general principles for additional alleles. A buried cluster of acidic amino acids in the binding groove predicted to be conserved among all murine I-E and human DR MHC class II molecules suggests how pH may influence MHC binding or exchange of peptides. These structures also complement mutational studies on the importance of individual peptide residues to T cell receptor recognition.