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1qrn

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1qrn, resolution 2.80Å ()
Domains: DUF1968, IGv, V-set, IGc, MHC_I
Related: 1ao7
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

Publication Abstract from PubMed

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.

Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical., Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC, Immunity. 1999 Jul;11(1):45-56. PMID:10435578

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1QRN is a 5 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Ding YH, Baker BM, Garboczi DN, Biddison WE, Wiley DC. Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Immunity. 1999 Jul;11(1):45-56. PMID:10435578

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