In vitro peptide binding to the heavy chain of the class I molecule of the major histocompatibility complex molecule HLA-A2.
In vitro peptide binding to the heavy chain of the class I molecule of the major histocompatibility complex molecule HLA-A2.
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DOI：
10.1073/pnas.88.4.1335
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发表时间：
1991-02
影响因子：
11.1
通讯作者：
Klaus Dornmair;Brian R. Clark;Harden M Mcconnell
中科院分区：
文献类型：
--
作者：
Klaus Dornmair;Brian R. Clark;Harden M Mcconnell
主要组织相容性复合体的I类分子的重链形成抗原肽的结合位点。我们描述了合成肽与人主要组织相容性复合体分子HLA-A2的纯化重链的结合。如果蛋白质首先通过在去污剂中还原其二硫键而部分变性，然后通过再氧化而复性，则发现肽结合能力显着增加。在某些去污剂的存在下，即使蛋白质部分解折叠，重链也能与肽结合。
The heavy chain of class I molecules of the major histocompatibility complex forms the binding site for antigenic peptides. We describe the binding of a synthetic peptide to the purified heavy chain of the human major histocompatibility complex molecule HLA-A2. The peptide binding capacity is found to be markedly increased if the protein is first partly denatured by reduction of its disulfide bonds in detergent and subsequently renatured by reoxidation. In the presence of certain detergents, the heavy chain binds peptides even when the protein is partly unfolded.