1I7U

CRYSTAL STRUCTURE OF CLASS I MHC A2 IN COMPLEX WITH PEPTIDE P1049-6V

Summary for 1I7U

• Entry DOI: 10.2210/pdb1i7u/pdb
• Related: 1I7R 1I7T
• Descriptor: HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, A-2 ALPHA CHAIN, BETA-2-MICROGLOBULIN, 9 RESIDUE PEPTIDE, ... (4 entities in total)
• Functional Keywords: mhc fold, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01892
• Total number of polymer chains: 6
• Total formula weight: 89469.56

Authors

Busslep, J.,Zhao, R.,Loftus, D.,Appella, E.,Collins, E.J. (deposition date: 2001-03-10, release date: 2001-10-24, Last modification date: 2024-10-30)

Primary citation

Busslep, J.,Zhao, R.,Donnini, D.,Loftus, D.,Saad, M.,Appella, E.,Collins, E.J.
T cell activity correlates with oligomeric peptide-major histocompatibility complex binding on T cell surface
J.Biol.Chem., 276:47320-47328, 2001

PubMed Abstract: Recognition of virally infected cells by CD8+ T cells requires differentiation between self and nonself peptide-class I major histocompatibility complexes (pMHC). Recognition of foreign pMHC by host T cells is a major factor in the rejection of transplanted organs from the same species (allotransplant) or different species (xenotransplant). AHIII12.2 is a murine T cell clone that recognizes the xenogeneic (human) class I MHC HLA-A2.1 molecule (A2) and the syngeneic murine class I MHC H-2 D(b) molecule (D(b)). Recognition of both A2 and D(b) are peptide-dependent, and the sequences of the peptides recognized have been determined. Alterations in the antigenic peptides bound to A2 cause large changes in AHIII12.2 T cell responsiveness. Crystal structures of three representative peptides (agonist, null, and antagonist) bound to A2 partially explain the changes in AHIII12.2 responsiveness. Using class I pMHC octamers, a strong correlation is seen between T cell activity and the affinity of pMHC complexes for the T cell receptor. However, contrary to previous studies, we see similar half-lives for the pMHC multimers bound to the AHIII12.2 cell surface.

PubMed: 11584024
DOI: 10.1074/jbc.M109231200

Experimental method

X-RAY DIFFRACTION (1.8 Å)