5c3t
From Proteopedia
PD-1 binding domain from human 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] Publication Abstract from PubMedTargeting 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. Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1.,Zak KM, Kitel R, Przetocka S, Golik P, Guzik K, Musielak B, Domling A, Dubin G, Holak TA Structure. 2015 Oct 22. pii: S0969-2126(15)00402-5. doi:, 10.1016/j.str.2015.09.010. PMID:26602187[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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