1.CAS Key Laboratory of
Pathogenic Microbiology and Immunology, Institute of Microbiology,
Chinese Academy of Sciences (CASPMI), Beijing 100101, China；College of Life Sciences,
Graduate University, Chinese Academy of Sciences, Beijing 100049,
China；China-Japan Joint Laboratory
of Molecular Immunology and Molecular Microbiology, Institute of Microbiology,
Chinese Academy of Sciences, Beijing 100101, China; 2.CAS Key Laboratory of
Pathogenic Microbiology and Immunology, Institute of Microbiology,
Chinese Academy of Sciences (CASPMI), Beijing 100101, China；College of Life Sciences,
Graduate University, Chinese Academy of Sciences, Beijing 100049,
China; 3.Institute of Biophysics,
Chinese Academy of Sciences, Beijing 100101, China; 4.CAS Key Laboratory of
Pathogenic Microbiology and Immunology, Institute of Microbiology,
Chinese Academy of Sciences (CASPMI), Beijing 100101, China; 5.CAS Key Laboratory of
Pathogenic Microbiology and Immunology, Institute of Microbiology,
Chinese Academy of Sciences (CASPMI), Beijing 100101, China；College of Life Sciences,
Graduate University, Chinese Academy of Sciences, Beijing 100049,
China；China-Japan Joint Laboratory
of Molecular Immunology and Molecular Microbiology, Institute of Microbiology,
Chinese Academy of Sciences, Beijing 100101, China；Beijing Institutes of
Life Science, Chinese Academy of Sciences, Beijing 100101, China;
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History+
Published Online
2010-02-01
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(367KB)
Abstract
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 C2221 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.
Yong Chen, Peipei Liu, Hao Cheng, Feng Gao, Jianxun Qi, George F. Gao,.
A dimeric structure of PD-L1: functional units
or evolutionary relics?.
Protein Cell, 2010, 1(2): 153-160 DOI:10.1007/s13238-010-0022-1
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(367KB)
