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7CGW

Complex structure of PD-1 and tislelizumab Fab

Summary for 7CGW
Entry DOI10.2210/pdb7cgw/pdb
DescriptorHeavy chain of tislelizumab Fab, Light chain of tislelizumab Fab, Programmed cell death protein 1, ... (4 entities in total)
Functional Keywordstislelizumab, pd-1, antibody, antitumor protein
Biological sourceHomo sapiens
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Total number of polymer chains6
Total formula weight131561.07
Authors
Hong, Y.,Feng, Y.C.,Liu, Y. (deposition date: 2020-07-02, release date: 2021-04-07, Last modification date: 2024-11-13)
Primary citationHong, Y.,Feng, Y.,Sun, H.,Zhang, B.,Wu, H.,Zhu, Q.,Li, Y.,Zhang, T.,Zhang, Y.,Cui, X.,Li, Z.,Song, X.,Li, K.,Liu, M.,Liu, Y.
Tislelizumab uniquely binds to the CC' loop of PD-1 with slow-dissociated rate and complete PD-L1 blockage.
Febs Open Bio, 11:782-792, 2021
Cited by
PubMed Abstract: Programmed cell death protein 1 (PD-1), an immune checkpoint receptor expressed by activated T, B, and NK cells, is a well-known target for cancer immunotherapy. Tislelizumab (BGB-A317) is an anti-PD-1 antibody that has recently been approved for treatment of Hodgkin's lymphoma and urothelial carcinoma. Here, we show that tislelizumab displayed remarkable antitumor efficacy in a B16F10/GM-CSF mouse model. Structural biology and Surface plasmon resonance (SPR) analyses revealed unique epitopes of tislelizumab, and demonstrated that the CC' loop of PD-1, a region considered to be essential for binding to PD-1 ligand 1 (PD-L1) but not reported as targeted by other therapeutic antibodies, significantly contributes to the binding of tislelizumab. The binding surface of tislelizumab on PD-1 overlaps largely with that of the PD-L1. SPR analysis revealed the extremely slow dissociation rate of tislelizumab from PD-1. Both structural and functional analyses align with the observed ability of tislelizumab to completely block PD-1/PD-L1 interaction, broadening our understanding of the mechanism of action of anti-PD-1 antibodies.
PubMed: 33527708
DOI: 10.1002/2211-5463.13102
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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