PEPTIDE BINDING AND PRESENTATION BY MOUSE CD1
PEPTIDE BINDING AND PRESENTATION BY MOUSE CD1
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DOI：
10.1126/science.7542403
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发表时间：
1995-07-14
期刊：
影响因子：
56.9
通讯作者：
PETERSON, PA
中科院分区：
文献类型：
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作者：
CASTANO, AR;TANGRI, S;PETERSON, PA
CD1分子与主要组织相容性复合体（MHC）Ⅰ类蛋白有远亲关系。它们的功能未知。用可溶性空载小鼠CD1（mCD1）对随机肽噬菌体展示文库进行筛选，确定了一个肽结合基序。它由三个被芳香族或大体积疏水氨基酸占据的锚定位点组成。平衡结合研究表明，mCD1以相对较高的亲和力结合含有合适基序的肽。然而，与经典的MHCⅠ类分子不同，与mCD1的强结合需要相对较长的肽。可以引发肽特异性的、受mCD1限制的T细胞应答，这表明这些发现具有免疫学意义。
CD1 molecules are distantly related to the major histocompatibility complex (MHC) class proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids, Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.