1B0G

CLASS I HISTOCOMPATIBILITY ANTIGEN (HLA-A2.1)/BETA 2-MICROGLOBULIN/PEPTIDE P1049 COMPLEX

Replaces:  1A9K

Summary for 1B0G

• Entry DOI: 10.2210/pdb1b0g/pdb
• Descriptor: CLASS I HISTOCOMPATIBILITY ANTIGEN, BETA 2-MICROGLOBULIN, PEPTIDE P1049 (ALWGFFPVL), ... (4 entities in total)
• Functional Keywords: class i histocompatibility antigen (hla-a2.1)-beta 2-microglobulin-peptide p1049 complex, histocompatibility antigen
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892; Secreted: P61769
• Total number of polymer chains: 6
• Total formula weight: 89565.64

Authors

Zhao, R.,Collins, E.J. (deposition date: 1998-11-09, release date: 1998-11-18, Last modification date: 2023-08-09)

Primary citation

Zhao, R.,Loftus, D.J.,Appella, E.,Collins, E.J.
Structural evidence of T cell xeno-reactivity in the absence of molecular mimicry.
J.Exp.Med., 189:359-370, 1999

PubMed Abstract: The T cell receptor (TCR), from a xeno-reactive murine cytotoxic T lymphocyte clone AHIII12.2, recognizes murine H-2Db complexed with peptide p1027 (FAPGVFPYM), as well as human HLA-A2.1 complexed with peptide p1049 (ALWGFFPVL). A commonly proposed model (the molecular mimicry model) used to explain TCR cross-reactivity suggests that the molecular surfaces of the recognized complexes are similar in shape, charge, or both, in spite of the primary sequence differences. To examine the mechanism of xeno-reactivity of AHIII12.2, we have determined the crystal structures of A2/p1049 and Db/p1027 to 2.5 A and 2.8 A resolution, respectively. The crystal structures show that the TCR footprint regions of the two class I complexes are significantly different in shape and charge. We propose that rather than simple molecular mimicry, unpredictable arrays of common and differential contacts on the two class I complexes are used for their recognition by the same TCR.

PubMed: 9892618
DOI: 10.1084/jem.189.2.359

Experimental method

X-RAY DIFFRACTION (2.5 Å)