Crystal structure of the beta chain of a T cell antigen receptor.
The crystal structure of the extracellular portion of the beta chain of a murine T cell antigen receptor (TCR), determined at a resolution of 1.7 angstroms, shows structural homology to immunoglobulins. The structure of the first and second hypervariable loops suggested that, in general, they adopt more restricted sets of conformations in TCR beta chains than those found in immunoglobulins; the third hypervariable loop had certain structural characteristics in common with those of immunoglobulin heavy chain variable domains. The variable and constant domains were in close contact, presumably restricting the flexibility of the beta chain. This may facilitate signal transduction from the TCR to the associated CD3 molecules in the TCR-CD3 complex.
Bentley
G A
GA
Unite d'Immunologie Structurale (CNRS URA 359), Institut Pasteur, Paris, France.
Boulot
G
G
Karjalainen
K
K
Mariuzza
R A
RA
D000595:Amino Acid Sequence; D000818:Animals; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D007135:Immunoglobulin Variable Region / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017260:Receptor-CD3 Complex, Antigen, T-Cell / Q000737:chemistry; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000737:chemistry*; D016415:Sequence Alignment; D015398:Signal Transduction
D007135:Immunoglobulin Variable Region; D017260:Receptor-CD3 Complex, Antigen, T-Cell; D016693:Receptors, Antigen, T-Cell, alpha-beta