Summary
PDB 1FYT deposited: 2000-10-03 modified: 2011-07-13
Title CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1
Authors Carfi, A., Hennecke, J., Wiley, D.C.
Method X-RAY DIFFRACTION
Structure factors resolution 2.6 rfactor 0.221 rfree 0.255
DPI 0.77 theoretical min: 0.39
Citations

An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA) peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to increase the local concentration of the interacting proteins once the peptide has been loaded onto the major histocompatibility complex (MHC) molecule. The structure of the complex, determined by X-ray crystallography, has a binding mode similar to that of the human B7 alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted are at the same positions observed earlier in class I MHC/peptide/TCR complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the response to HA/HLA-DR appears to conserve charged interactions between three lysines of the peptide and acidic residues on the TCR.

EMBO J. 2000 Nov 1;19(21):5611-24.

Cross References
Database source Identifier Description
PubMed 11060013 EMJODG
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1FYT/1 1FYT 1 pentamer 0 5 2 6133