PDBsum entry 1qrn

Immune system

PDB id: 1qrn

Contents

Protein chains

274 a.a. *

100 a.a. *

200 a.a. *

243 a.a. *

Ligands

LEU-LEU-PHE-GLY-TYR-ALA-VAL-TYR-VAL

Waters ×51

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Four a6-Tcr/peptide/hla-A2 structures that generate very different t cell signals are nearly identical.

Authors

Y.H.Ding, B.M.Baker, D.N.Garboczi, W.E.Biddison, D.C.Wiley.

Ref.

Immunity, 1999, 11, 45-56. [DOI no: 10.1016/S1074-7613(00)80080-1]

PubMed id

10435578

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.

Figure 3.

Figure 4.

The above figures are reprinted by permission from Cell Press: Immunity (1999, 11, 45-56) copyright 1999.

Secondary reference #1

Title

Structure of the complex between human t-Cell receptor, Viral peptide and hla-A2.

Authors

D.N.Garboczi, P.Ghosh, U.Utz, Q.R.Fan, W.E.Biddison, D.C.Wiley.

Ref.

Nature, 1996, 384, 134-141.

PubMed id

8906788