期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1992
卷号:89
期号:24
页码:12117-12121
DOI:10.1073/pnas.89.24.12117
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Transfected Drosophila melanogaster cells can express large quantities of class I major histocompatibility complex molecules. Such molecules lack endogenous peptides because the Drosophila cells are devoid of proteins necessary for intracellular peptide loading. The empty molecules are efficiently expressed on the cell surface and can acquire extracellular peptides. The conformation and stability of empty murine class I molecules are determined by the source of beta 2-microglobulin. All beta 2-microglobulin-induced conformers of empty heavy chains seem to be unified in a common rigid conformation on peptide binding.