Journal
STRUCTURE
Volume 25, Issue 8, Pages 1163-1174Publisher
CELL PRESS
DOI: 10.1016/j.str.2017.06.011
Keywords
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Funding
- National Science Centre, Poland [UMO-2016/20/T/NZ1/00519, UMO-2015/19/D/NZ1/02009, UMO-2012/06/A/ST5/00224, UMO-2014/12/W/NZ1/00457]
- Seventh European Community Framework Programme
- NIH [2R01GM097082-05]
- Kanker Bestrijding [KWF-10504]
- Innovative Medicines Initiative [115489]
- European Union's Seventh Framework Programme
- EFPIA
- European Union's Horizon research and innovation programme under MSCITN [675555]
- CoFund ALERT [665250]
- National Science Center [UMO-2012/07/E/NZ1/01907]
- Faculty of Biochemistry, Biophysics and Biotechnology of Jagiellonian University
- Ministry of Science and Higher Education
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Cancer cells can avoid and suppress immune responses through activation of inhibitory immune checkpoint proteins, such as PD-1, PD-L1, and CTLA-4. Blocking the activities of these proteins with monoclonal antibodies, and thus restoring T cell function, has delivered breakthrough therapies against cancer. In this review, we describe the latest work on structural characterization of the checkpoint proteins, their interactions with cognate ligands and with therapeutic antibodies. Structures of the extracellular portions of these proteins reveal that they all have a similar modular structure, composed of small domains similar in topology to the domains found in antibodies. Structural basis for blocking the PD-1/PD-L1 interaction by small molecules is illustrated with the compound BMS-202 that binds to and induces dimerization of PD-L1.
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