3FN3

Dimeric Structure of PD-L1

Summary for 3FN3

• Entry DOI: 10.2210/pdb3fn3/pdb
• Descriptor: Programmed cell death 1 ligand 1 (1 entity in total)
• Functional Keywords: b7-h1, pd-l1, programmed cell death 1, cell membrane, glycoprotein, immunoglobulin domain, membrane, receptor, transmembrane, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Endomembrane system; Single-pass type I membrane protein: Q9NZQ7
• Total number of polymer chains: 2
• Total formula weight: 50711.59

Authors

Chen, Y.,Gao, F.,Liu, P.,Chu, F.,Qi, J.,Gao, G.F. (deposition date: 2008-12-23, release date: 2009-12-29, Last modification date: 2024-10-30)

Primary citation

Chen, Y.,Liu, P.,Gao, F.,Cheng, H.,Qi, J.,Gao, G.F.
A dimeric structure of PD-L1: functional units or evolutionary relics?
Protein Cell, 1:153-160, 2010

PubMed 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 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.

PubMed: 21203985
DOI: 10.1007/s13238-010-0022-1

Experimental method

X-RAY DIFFRACTION (2.7 Å)