1QRN

CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A

Summary for 1QRN

• Entry DOI: 10.2210/pdb1qrn/pdb
• Related: 1AO7
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, BETA-2 MICROGLOBULIN, TAX PEPTIDE P6A, ... (6 entities in total)
• Functional Keywords: human tcr-peptide-mhc complex, hla-a2, htlv-1, tax, tcr, t cell receptor, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769; Membrane; Single-pass membrane protein (Potential): P01848
• Total number of polymer chains: 5
• Total formula weight: 93954.15

Authors

Ding, Y.H.,Baker, B.M.,Garboczi, D.N.,Biddison, W.E.,Wiley, D.C. (deposition date: 1999-06-14, release date: 1999-10-14, Last modification date: 2024-10-30)

Primary citation

Ding, Y.H.,Baker, B.M.,Garboczi, D.N.,Biddison, W.E.,Wiley, D.C.
Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical.
Immunity, 11:45-56, 1999

PubMed Abstract: The interactions of three singly substituted peptide variants of the HTLV-1 Tax peptide bound to HLA-A2 with the A6 T cell receptor have been studied using T cell assays, kinetic and thermodynamic measurements, and X-ray crystallography. The three peptide/MHC ligands include weak agonists and antagonists with different affinities for TCR. The three-dimensional structures of the three A6-TCR/peptide/HLA-A2 complexes are remarkably similar to each other and to the wild-type agonist complex, with minor adjustments at the interface to accommodate the peptide substitutions (P6A, V7R, and Y8A). The lack of correlation between structural changes and the type of T cell signals induced provides direct evidence that different signals are not generated by different ligand-induced conformational changes in the alphabeta TCR.

PubMed: 10435578
DOI: 10.1016/S1074-7613(00)80080-1

Experimental method

X-RAY DIFFRACTION (2.8 Å)