Fahnestock M L, Tamir I, Narhi L, Bjorkman P J
Division of Biology, California Institute of Technology, Pasadena 91125.
Science. 1992 Dec 4;258(5088):1658-62. doi: 10.1126/science.1360705.
A secreted form of a class I major histocompatibility complex (MHC) molecule was denatured and renatured in vitro in the absence of peptide. The resulting empty class I heterodimer was immunologically reactive and structurally similar to a heterodimer renatured in the presence of an appropriate restricted peptide. Thermal stability profiles indicated that the two forms of heterodimer differed in their resistance to denaturation by heat but that a significant portion of the empty class I heterodimers had a native conformation at physiological temperatures. Free energies calculated from these data gave a direct measure of the stabilization of the class I MHC molecule that resulted from peptide binding.
