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T Cell Receptor Signaling Is Limited by Docking Geometry to Peptide-Major Histocompatibility Complex
Open accessAbstract
T cell receptor (TCR) engagement of peptide-major histocompatibility complex (MHC) is essential to adaptive immunity, but it is unknown if TCR signaling responses are influenced by the binding topology of the TCR-peptide-MHC complex. We developed yeast-displayed peptide-MHC libraries that enabled us to identify new peptide sequences reactive with a single TCR. Structural analysis showed that four peptides bound to the TCR with distinct 3-dimensional (3D) and 2D affinities, using entirely different binding chemistries. Three of the peptides that shared a common docking mode, where key TCR-MHC germline interactions are preserved, induced TCR signaling. The fourth peptide failed to induce signaling, and was recognized in a substantially different TCR-MHC binding mode that apparently exceeded geometric tolerances compatible with signaling. We suggest that the ‘stereotypical’ TCR-MHC docking paradigm evolved from productive signaling geometries, and that TCR signaling can be modulated by peptides that are recognized in alternative TCR-pMHC binding orientations.
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Cited by
Optogenetic control shows that kinetic proofreading regulates the activity of the T cell receptor
Yousefi, O. S., Günther, M., Hörner, M., Chalupsky, J., Wess, M., Brandl, S. M., Smith, R. W., Fleck, C., Kunkel, T., Zurbriggen, M. D., et al. (2019) · eLife · doi:10.7554/elife.42475 · Cited by 117
TCR catch bonds nonlinearly control CD8 cooperation to shape T cell specificity
Qin, R., Zhang, Y., Shi, J., Wu, P., An, C., Li, Z., Liu, N., Wan, Z., Hua, T., Li, X., et al. (2025) · Cell Research · doi:10.1038/s41422-025-01077-9 · Cited by 35
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Metadata
- Authors
- Adams, J. J., Narayanan, S., Liu, B., Birnbaum, M. E., Kruse, A. C., Bowerman, N. A., Chen, W., Levin, A. M., Connolly, J. M., Zhu, C., Kranz, D. M., & Garcia, K. C.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2011-11
- Volume
- 35
- Issue
- 5
- Pages
- 681-693
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2038509173
- Cited by
- 253
- References
- 0
- FWCI
- 9.20
- Type
- journal article
- Language
- en
- Open access
- bronze
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