Abstract
Using NMR spectroscopy, we determined the solution structure of a single-chain T-cell receptor (scTCR) derived from the major histocompatibility complex (MHC) class II-restricted D10 TCR. The conformations of complementarity-determining regions (CDRs) 3beta and 1alpha and surface properties of 2alpha are different from those of related class I-restricted TCRs. We infer a conserved orientation for TCR V(alpha) domains in complexes with both class I and II MHC-peptide ligands, which implies that small structural variations in V(alpha) confer MHC class preference. High mobility of CDR3 residues relative to other CDR or framework residues (picosecond time scale) provides insight into immune recognition and selection mechanisms.
Publication types
-
Comparative Study
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Binding Sites
-
Conserved Sequence
-
Histocompatibility Antigens Class I / immunology
-
Histocompatibility Antigens Class II / immunology*
-
Humans
-
Kinetics
-
Ligands
-
Models, Molecular
-
Molecular Sequence Data
-
Nuclear Magnetic Resonance, Biomolecular
-
Protein Binding
-
Protein Conformation
-
Protein Structure, Secondary
-
Receptors, Antigen, T-Cell / chemistry*
-
Receptors, Antigen, T-Cell / immunology*
-
Receptors, Antigen, T-Cell / metabolism
-
Recombinant Fusion Proteins / chemistry
-
Recombinant Fusion Proteins / metabolism
-
Sequence Alignment
-
Solubility
-
Thermodynamics
Substances
-
Histocompatibility Antigens Class I
-
Histocompatibility Antigens Class II
-
Ligands
-
Receptors, Antigen, T-Cell
-
Recombinant Fusion Proteins