3fn3
Dimeric Structure of PD-L1
Structural highlights
FunctionPD1L1_HUMAN Involved in the costimulatory signal, essential for T-cell proliferation and production of IL10 and IFNG, in an IL2-dependent and a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation and cytokine production.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPD-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. A dimeric structure of PD-L1: functional units or evolutionary relics?,Chen Y, Liu P, Gao F, Cheng H, Qi J, Gao GF Protein Cell. 2010 Feb;1(2):153-60. Epub 2010 Feb 6. PMID:21203985[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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