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Quantifying conformational changes in the TCR:pMHC-I binding interface.

Benjamin McMaster^1,2, Christopher J Thorpe^3,4, Jamie Rossjohn^5,6

¹Koohy Lab, Medical Research Council Translational Immune Discovery Unit (MRC TIDU), Weatherall Institute of Molecular Medicine (WIMM), Radcliffe Department of Medicine, University of Oxford, Oxford, United Kingdom.

Frontiers in Immunology

|December 17, 2024

Summary

This summary is machine-generated.

T cell antigen receptor (TCR) interactions with peptide-MHC class I (pMHC-I) involve conformational changes, particularly in CDR3 loops, influencing T cell recognition and antigen specificity modeling.

Keywords:

HLA MHC T cell antigen specificity TCR conformational changes peptide structural biology

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Area of Science:

Immunology
Structural Biology
Computational Biology

Background:

T cells are crucial for adaptive immunity, recognizing antigens via T cell receptors (TCRs) interacting with peptide-MHC (pMHC) molecules.
The conformational dynamics of the TCR:pMHC interface are critical for T cell activation but remain incompletely understood.
Previous studies on TCR:pMHC-I interactions yielded mixed results regarding interface conformational changes, lacking broad statistical validation.

Purpose of the Study:

To quantitatively analyze conformational changes within the TCR:pMHC-I binding interface.
To elucidate the specific regions of TCRs and pMHC-Is that undergo conformational modifications upon binding.
To establish a structural basis for understanding T cell antigen specificity.

Main Methods:

Compiled a dataset of 391 structures, including 22 TCRs, 19 MHC alleles, and 79 peptides in both unbound (apo) and bound (holo) states.
Analyzed structural data to quantify conformational alterations in the TCR:pMHC-I complex.
Mapped intermolecular contacts to identify key binding interfaces and interaction patterns.

Main Results:

All complementarity-determining region (CDR) loops exhibit some movement; CDR3α and CDR3β loops significantly alter their shape upon pMHC-I binding.
A novel TCR:pMHC-I interaction fingerprint was generated, showing CDR3α binding the peptide N-terminus and CDR3β binding the C-terminus.
Peptide conformational changes occur upon TCR engagement, with the extent depending on peptide anchoring within the MHC binding groove.

Conclusions:

TCR:pMHC-I binding involves dynamic conformational changes in CDR loops and peptides, crucial for T cell recognition.
The findings provide insights into T cell antigen specificity mechanisms.
This work aids in developing computational models for predicting T cell antigen specificity, addressing a major challenge in immunology.