1FYT

CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1

Summary for 1FYT

• Entry DOI: 10.2210/pdb1fyt/pdb
• Related: 1DLH
• Descriptor: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR-1 BETA CHAIN, HEMAGGLUTININ HA1 PEPTIDE CHAIN, ... (7 entities in total)
• Functional Keywords: protein-protein complex, immunoglobulin fold, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 96710.28

Authors

Hennecke, J.,Carfi, A.,Wiley, D.C. (deposition date: 2000-10-03, release date: 2000-11-08, Last modification date: 2024-10-30)

Primary citation

Hennecke, J.,Carfi, A.,Wiley, D.C.
Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1.
EMBO J., 19:5611-5624, 2000

PubMed Abstract: 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.

PubMed: 11060013
DOI: 10.1093/emboj/19.21.5611

Experimental method

X-RAY DIFFRACTION (2.6 Å)