5C3T
PD-1 binding domain from human PD-L1
Summary for 5C3T
| Entry DOI | 10.2210/pdb5c3t/pdb |
| Related | 4ZQK |
| Descriptor | Programmed cell death 1 ligand 1 (2 entities in total) |
| Functional Keywords | immunology, ligand, pd1/pdl1 axis, 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 | 1 |
| Total formula weight | 14403.45 |
| Authors | Zak, K.M.,Dubin, G.,Holak, T.A. (deposition date: 2015-06-17, release date: 2015-11-04, Last modification date: 2024-10-16) |
| Primary citation | Zak, K.M.,Kitel, R.,Przetocka, S.,Golik, P.,Guzik, K.,Musielak, B.,Domling, A.,Dubin, G.,Holak, T.A. Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1. Structure, 23:2341-2348, 2015 Cited by PubMed Abstract: Targeting the PD-1/PD-L1 immunologic checkpoint with monoclonal antibodies has recently provided breakthrough progress in the treatment of melanoma, non-small cell lung cancer, and other types of cancer. Small-molecule drugs interfering with this pathway are highly awaited, but their development is hindered by insufficient structural information. This study reveals the molecular details of the human PD-1/PD-L1 interaction based on an X-ray structure of the complex. First, it is shown that the ligand binding to human PD-1 is associated with significant plasticity within the receptor. Second, a detailed molecular map of the interaction surface is provided, allowing definition of the regions within both interacting partners that may likely be targeted by small molecules. PubMed: 26602187DOI: 10.1016/j.str.2015.09.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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