1BWM
A SINGLE-CHAIN T CELL RECEPTOR
Summary for 1BWM
| Entry DOI | 10.2210/pdb1bwm/pdb |
| Descriptor | PROTEIN (ALPHA-BETA T CELL RECEPTOR (TCR) (D10)) (1 entity in total) |
| Functional Keywords | immunoglobulin, immunoreceptor, immune system |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 26970.66 |
| Authors | Hare, B.J.,Wyss, D.F.,Reinherz, E.L.,Wagner, G. (deposition date: 1998-09-23, release date: 1999-07-22, Last modification date: 2024-10-30) |
| Primary citation | Hare, B.J.,Wyss, D.F.,Osburne, M.S.,Kern, P.S.,Reinherz, E.L.,Wagner, G. Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor. Nat.Struct.Biol., 6:574-581, 1999 Cited by PubMed 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. PubMed: 10360364DOI: 10.1038/9359 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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