What do TCR–pMHC crystal structures teach us about MHC restriction and alloreactivity?
- 1 August 2003
- journal article
- review article
- Published by Elsevier in Trends in Immunology
- Vol. 24 (8) , 429-437
- https://doi.org/10.1016/s1471-4906(03)00180-7
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- CDR3 loop flexibility contributes to the degeneracy of TCR recognitionNature Immunology, 2003
- Structure of a Complex of the Human α/β T Cell Receptor (TCR) HA1.7, Influenza Hemagglutinin Peptide, and Major Histocompatibility Complex Class II Molecule, HLA-DR4 (DRA0101 and DRB10401)The Journal of Experimental Medicine, 2002
- Identification of a Crucial Energetic Footprint on the α1 Helix of Human Histocompatibility Leukocyte Antigen (Hla)-A2 That Provides Functional Interactions for Recognition by Tax Peptide/Hla-A2–Specific T Cell ReceptorsThe Journal of Experimental Medicine, 2001
- Role of 2c T Cell Receptor Residues in the Binding of Self–And Allo–Major Histocompatibility ComplexesThe Journal of Experimental Medicine, 2000
- Canonical structures for the hypervariable regions of T cell αβ receptorsJournal of Molecular Biology, 2000
- How Many Thymocytes Audition for Selection?The Journal of Experimental Medicine, 1997
- The MHC Reactivity of the T Cell Repertoire Prior to Positive and Negative SelectionCell, 1997
- Structure of the Transition State for Folding of a Protein Derived from Experiment and SimulationJournal of Molecular Biology, 1996
- Characterizing transition states in protein folding: an essential step in the puzzleCurrent Opinion in Structural Biology, 1995
- High determinant density may explain the phenomenon of alloreactivityImmunology Today, 1984