Bjorkman P J, Saper M A, Samraoui B, Bennett W S, Strominger J L, Wiley D C
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts.
Nature. 1987;329(6139):512-8. doi: 10.1038/329512a0.
Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.
I类组织相容性抗原HLA - A2的大多数多态性氨基酸聚集在分子顶部的一个大沟中，该沟被确定为加工后外来抗原的识别位点。许多对HLA的T细胞识别至关重要的残基位于该位点，其位置使其能够作为加工后抗原的配体。这些发现对主要组织相容性复合体（MHC）的产物如何识别外来抗原具有启示意义。
