Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor

摘要: Using NMR spectroscopy, we determined the solution structure of a single-chain T-cell receptor (scTCR) derived from major histocompatibility complex (MHC) class II-restricted D10 TCR. The conformations complementarity-determining regions (CDRs) 3β and 1α surface properties 2α are different those related I-restricted TCRs. We infer conserved orientation for TCR Vα domains in complexes with both I II MHC–peptide ligands, which implies that small structural variations confer MHC preference. High mobility CDR3 residues relative to other CDR or framework (picosecond time scale) provides insight into immune recognition selection mechanisms.