CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences (CASPMI), Beijing 100101, China.
Protein Cell. 2010 Feb;1(2):153-60. doi: 10.1007/s13238-010-0022-1. Epub 2010 Feb 6.
PD-L1 is a member of the B7 protein family, most of whose members so far were identified as dimers in a solution and crystalline state, either complexed or uncomplexed with their ligand(s). The binding of PD-L1 with its receptor PD-1 (CD279) delivers an inhibitory signal regulating the T cell function. Simultaneously with the Garboczi group, we successfully solved another structure of human PD-L1 (hPD-L1). Our protein crystallized in the space group of C222(1) with two hPD-L1 molecules per asymmetric unit. After comparison of reported B7 structures, we have found some intrinsic factors involved in the interaction of these two molecules. Based on these results, we tend to believe this uncomplexed hPD-L1 structure demonstrated its potential dimeric state in solution, although it could just be an evolutionary relic, too weak to be detected under present technology, or still a functional unit deserved our attentions.
PD-L1 是 B7 蛋白家族的一员,到目前为止,其大多数成员在溶液和结晶状态下被鉴定为二聚体,无论是与配体结合还是未结合。PD-L1 与其受体 PD-1(CD279)的结合传递调节 T 细胞功能的抑制信号。与 Garboczi 小组同时,我们成功解决了另一个人源 PD-L1(hPD-L1)的结构。我们的蛋白质在 C222(1)空间群中结晶,每个不对称单位有两个 hPD-L1 分子。在比较报告的 B7 结构后,我们发现了一些涉及这两个分子相互作用的内在因素。基于这些结果,我们倾向于认为这种未结合的 hPD-L1 结构在溶液中表现出其潜在的二聚体状态,尽管它可能只是一种进化遗迹,太弱以至于无法在现有技术下检测到,或者仍然是一个值得我们关注的功能单元。