ArticleMethods in molecular biology (Clifton, N.J.)2026
Method for Performing T Cell Receptor-Peptide-Human Leukocyte Antigen Co-complexation and Structural Analysis.
Article in Methods in molecular biology (Clifton, N.J.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Phosphorylation of a Tumor-Derived ASXL2 Epitope Remodels the HLA-Bound Peptide Conformational Ensemble and Interaction Network of the Peptide-HLA Complex.Computational and structural biotechnology journal · 2026Article
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Authors and funding
2 authors.
Funding
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Abstract
An important component of the adaptive immune system is the T cells that detect and clear pathogen-infected cells. T cells have surface receptors (TCRs) that recognize pathogen-derived peptides bound by immune proteins called Human Leukocyte Antigens (HLA) in humans. The intricate interaction between the TCR and the peptide-HLA (pHLA) complex drives the T cell activation that, in turn, dictates infection's outcome. To understand this key interaction, X-ray crystallography has been used to determine the atomic structures of both the TCR and the pHLA after complex formation. In this chapter, we describe the method to form a TCR-pHLA complex, crystallize it and analyze the resulting crystal structure.
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Registered trials
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