Back to Search
Start Over
Two human T cell receptors bind in a similar diagonal mode to the HLA-A2/Tax peptide complex using different TCR amino acids.
- Source :
-
Immunity [Immunity] 1998 Apr; Vol. 8 (4), pp. 403-11. - Publication Year :
- 1998
-
Abstract
- The three-dimensional structure of a human alphabeta T cell receptor (TCR), B7, bound to the HLA-A2 molecule/HTLV-1 Tax peptide complex was determined by x-ray crystallography. Although different from the A6 TCR, previously studied, in 16 of the 17 residues that contact HLA-A2/Tax, the B7 TCR binds in a similar diagonal manner, only slightly tipped and rotated, relative to the A6 TCR. The structure explains data from functional assays on the specificity differences between the B7 and A6 TCRs for agonist, partial agonist, and null peptides. The existence of a structurally similar diagonal binding mode for TCRs favors mechanisms based on the formation of geometrically defined supramolecular assemblies for initiating signaling.
- Subjects :
- Amino Acid Sequence
Amino Acid Substitution
Binding Sites genetics
Crystallography, X-Ray
Humans
In Vitro Techniques
Models, Molecular
Molecular Sequence Data
Protein Binding
Protein Conformation
Receptors, Antigen, T-Cell, alpha-beta genetics
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins metabolism
Signal Transduction
T-Lymphocytes immunology
Gene Products, tax metabolism
HLA-A2 Antigen metabolism
Receptors, Antigen, T-Cell, alpha-beta chemistry
Receptors, Antigen, T-Cell, alpha-beta metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1074-7613
- Volume :
- 8
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Immunity
- Publication Type :
- Academic Journal
- Accession number :
- 9586631
- Full Text :
- https://doi.org/10.1016/s1074-7613(00)80546-4