Structure of crossreactive human histocompatibility antigens HLA-A28 and HLA-A2: possible implications for the generation of HLA polymorphism.
Structure of crossreactive human histocompatibility antigens HLA-A28 and HLA-A2: possible implications for the generation of HLA polymorphism.
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交叉反应性人类组织相容性抗原 HLA-A28 和 HLA-A2 的结构：对 HLA 多态性产生的可能影响。
DOI：
10.1073/pnas.79.12.3813
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发表时间：
1982
影响因子：
11.1
通讯作者：
H. Orr
中科院分区：
文献类型：
--
作者：
J. A. López de Castro;J. Strominger;D. Strong;H. Orr
两种高度交叉反应的人类组织相容性抗原HLA-A28和HLA-A2的一级结构已分别确定为木瓜蛋白酶溶解分子的96%和90%。将它们的序列与HLA-B7的序列进行比较，并相互比较，以概述多样性的位点。HLA-B7与这些HLA-A抗原之间的总体同源性为86%。绝大多数差异位于残基43和195之间。在该区域内，取代聚集在至少三个区段中-残基65-80、105-116和177-194。HLA-A28与HLA-A2具有96%的同源性。大部分差异都在第65-74段和第107-116段。这些结果有力地支持了这样的建议，即这些片段中的残基是HLA-A28和HLA-A2的同种抗原决定簇的组成部分。有人进一步提出，这三个集群可能构成主要的，但不是唯一的，在人类组织相容性抗原的抗原多样性的网站。HLA-B7、HLA-A28和HLA-A2在第一可变片段中的差异的性质表明，基因转换可能在HLA多态性的产生中起一定作用。
The primary structure of two highly crossreactive human histocompatibility antigens, HLA-A28 and HLA-A2, has been determined to 96% and 90%, respectively, of the papain-solubilized molecules. Their sequences have been compared with the sequence of HLA-B7 and with each other in order to outline the sites of diversity. The overall homology between HLA-B7 and these HLA-A antigens is 86%. A large majority of the differences are located between residues 43 and 195. Within this area, substitutions cluster in at least three segments--residues 65-80, 105-116, and 177-194. HLA-A28 and HLA-A2 show 96% homology. Most of the differences fall within segments 65-74 and 107-116. These results strongly support the suggestion that residues in these segments are integral parts of the alloantigenic determinants of HLA-A28 and HLA-A2. It is further proposed that these three clusters may constitute major, albeit not exclusive, sites of antigenic diversity in human histocompatibility antigens. The nature of the differences among HLA-B7, HLA-A28, and HLA-A2 in the first variable segment suggests that gene conversion might play some role in the generation of HLA polymorphism.