人类I类组织相容性抗原HLA - A2的结构
Structure of the human class I histocompatibility antigen, HLA-A2.
作者信息
Bjorkman P J, Saper M A, Samraoui B, Bennett W S, Strominger J L, Wiley D C
机构信息
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
出版信息
Nature. 1987;329(6139):506-12. doi: 10.1038/329506a0.
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.
人类细胞膜上的I类组织相容性抗原具有两种结构基序：糖蛋白的膜近端包含两个具有免疫球蛋白折叠的结构域，它们以一种新颖的方式配对；远离膜的区域是一个由八个反平行β链组成的平台，顶部为α螺旋。α螺旋之间的一个大凹槽为加工后的外来抗原提供了一个结合位点。在纯化的HLA-A2晶体的这个位点发现了一种未知的“抗原”。
Zotero 插件