1FO0

MURINE ALLOREACTIVE SCFV TCR-PEPTIDE-MHC CLASS I MOLECULE COMPLEX

Summary for 1FO0

• Entry DOI: 10.2210/pdb1fo0/pdb
• Descriptor: PROTEIN (ALLOGENEIC H-2KB MHC CLASS I MOLECULE), PROTEIN (BETA-2 MICROGLOBULIN), NATURALLY PROCESSED OCTAPEPTIDE PBM1, ... (6 entities in total)
• Functional Keywords: t cell receptor, class i mhc, h-2kb, tcr-pmhc complex, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887
• Total number of polymer chains: 5
• Total formula weight: 70507.53

Authors

Reiser, J.B.,Darnault, C.,Guimezanes, A.,Gregoire, C.,Mosser, T.,Schmitt-Verhulst, A.-M.,Fontecilla-Camps, J.C.,Malissen, B.,Housset, D.,Mazza, G. (deposition date: 2000-08-24, release date: 2000-10-02, Last modification date: 2024-11-13)

Primary citation

Reiser, J.B.,Darnault, C.,Guimezanes, A.,Gregoire, C.,Mosser, T.,Schmitt-Verhulst, A.-M.,Fontecilla-Camps, J.C.,Malissen, B.,Housset, D.,Mazza, G.
Crystal structure of a T cell receptor bound to an allogeneic MHC molecule.
Nat.Immunol., 1:291-297, 2000

PubMed Abstract: Many T cell receptors (TCRs) that are selected to respond to foreign peptide antigens bound to self major histocompatibility complex (MHC) molecules are also reactive with allelic variants of self-MHC molecules. This property, termed alloreactivity, causes graft rejection and graft-versus-host disease. The structural features of alloreactivity have yet to be defined. We now present a basis for this cross-reactivity, elucidated by the crystal structure of a complex involving the BM3.3 TCR and a naturally processed octapeptide bound to the H-2Kb allogeneic MHC class I molecule. A distinguishing feature of this complex is that the eleven-residue-long complementarity-determining region 3 (CDR3) found in the BM3.3 TCR alpha chain folds away from the peptide binding groove and makes no contact with the bound peptide, the latter being exclusively contacted by the BM3.3 CDR3 beta. Our results formally establish that peptide-specific, alloreactive TCRs interact with allo-MHC in a register similar to the one they use to contact self-MHC molecules.

PubMed: 11017099
DOI: 10.1038/79728

Experimental method

X-RAY DIFFRACTION (2.5 Å)