Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1

Zak, K. M., Kitel, R., Przetocka, S., Golik, P., Guzik, K., Musielak, B., Dömling, A., Dubin, G. & Holak, T. A., 1-Dec-2015, In : Structure. 23, 12, p. 2341-2348 8 p.

Research output: Contribution to journalArticleAcademicpeer-review

  • Krzysztof M. Zak
  • Radoslaw Kitel
  • Sara Przetocka
  • Przemyslaw Golik
  • Katarzyna Guzik
  • Bogdan Musielak
  • Alexander Dömling
  • Grzegorz Dubin
  • Tad A. Holak
Summary 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.
Original languageEnglish
Pages (from-to)2341-2348
Number of pages8
Issue number12
Publication statusPublished - 1-Dec-2015


  • human programmed death 1, membrane protein, programmed death 1, programmed death 1 ligand 1, unclassified drug, article, conformational transition, crystal structure, ligand binding, priority journal, protein protein interaction, protein structure, stoichiometry

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