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Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
- Source :
- Nature. 384:134-141
- Publication Year :
- 1996
- Publisher :
- Springer Science and Business Media LLC, 1996.
-
Abstract
- Recognition by a T-cell antigen receptor (TCR) of peptide complexed with a major histocompatibility complex (MHC) molecule occurs through variable loops in the TCR structure which bury almost all the available peptide and a much larger area of the MHC molecule. The TCR fits diagonally across the MHC peptide-binding site in a surface feature common to all class I and class II MHC molecules, providing evidence that the nature of binding is general. A broadly applicable binding mode has implications for the mechanism of repertoire selection and the magnitude of alloreactions.
- Subjects :
- Models, Molecular
Protein Conformation
Receptors, Antigen, T-Cell
chemical and pharmacologic phenomena
Crystallography, X-Ray
Major histocompatibility complex
Major Histocompatibility Complex
T cell receptor binding
Protein structure
Antigen
HLA-A2 Antigen
MHC class I
Immune Tolerance
Humans
Immunoglobulin Fragments
Genetics
Human T-lymphotropic virus 1
Multidisciplinary
biology
T-cell receptor
Gene Products, tax
MHC restriction
Cell biology
biology.protein
Protein Binding
Signal Transduction
Subjects
Details
- ISSN :
- 14764687 and 00280836
- Volume :
- 384
- Database :
- OpenAIRE
- Journal :
- Nature
- Accession number :
- edsair.doi.dedup.....b792ef4c4118fa6155d9ff61be81b991
- Full Text :
- https://doi.org/10.1038/384134a0