Dornmair K, Clark B R, McConnell H M
Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.
Proc Natl Acad Sci U S A. 1991 Feb 15;88(4):1335-8. doi: 10.1073/pnas.88.4.1335.
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.
主要组织相容性复合体I类分子的重链形成抗原肽的结合位点。我们描述了一种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。如果首先通过在去污剂中还原其二硫键使蛋白质部分变性，随后通过再氧化使其复性，发现肽结合能力会显著增加。在某些去污剂存在的情况下，即使蛋白质部分展开，重链也能结合肽。
