Journal
PROTEIN & CELL
Volume 1, Issue 2, Pages 153-160Publisher
SPRINGEROPEN
DOI: 10.1007/s13238-010-0022-1
Keywords
PD-L1; crystal structure; dimer; costimulatory molecules; B7 family
Categories
Funding
- Ministry of Science and Technology (MOST) of China [2006CB504204]
- National Natural Science Foundation (NSFC) of China [30671903]
- Chinese Academy of Sciences (CAS) [KSCX2-SW-227]
- NSFC [30525010]
- Science Innovation Project, Graduate University of Chinese Academy of Sciences (GUCAS) [0729031EE1]
- Japan MEXT (Ministry of Education, Culture, Sports, Science and Technology)
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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, althougt it could just be an evolutionary relic, too weak to be detected under present technology, or still a functional unit deserved our attentions.
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