2QRS
Crystal Structure of a single chain trimer composed of the MHC I heavy chain H-2Kb Y84A, beta-2microglobulin, and ovalbumin-derived peptide.
Summary for 2QRS
| Entry DOI | 10.2210/pdb2qrs/pdb |
| Related | 2QRI 2QRT |
| Descriptor | H-2 class I histocompatibility antigen K-B alpha chain, Beta-2 microglobulin, ovalbumin-derived peptide (2 entities in total) |
| Functional Keywords | mhc-i, single chain, ovalbumin, glycoprotein, immune response, membrane, mhc i, transmembrane, immune system |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 2 |
| Total formula weight | 93948.55 |
| Authors | Mitaksov, V.E.,Fremont, D.H. (deposition date: 2007-07-29, release date: 2007-11-06, Last modification date: 2024-11-20) |
| Primary citation | Mitaksov, V.,Truscott, S.M.,Lybarger, L.,Connolly, J.M.,Hansen, T.H.,Fremont, D.H. Structural engineering of pMHC reagents for T cell vaccines and diagnostics. Chem.Biol., 14:909-922, 2007 Cited by PubMed Abstract: MHC class I peptide complexes (pMHC) are routinely used to enumerate T cell populations and are currently being evaluated as vaccines to tumors and specific pathogens. Herein, we describe the structures of three generations of single-chain pMHC progressively designed for the optimal presentation of covalently associated epitopes. Our ultimate design employs a versatile disulfide trap between an invariant MHC residue and a short C-terminal peptide extension. This general strategy is nondisruptive of native pMHC conformation and T cell receptor engagement. Indeed, cell-surface-expressed MHC complexes with disulfide-trapped epitopes are refractory to peptide exchange, suggesting they will make safe and effective vaccines. Furthermore, we find that disulfide-trap stabilized, recombinant pMHC reagents reliably detect polyclonal CD8 T cell populations as proficiently as conventional reagents and are thus well suited to monitor or modulate immune responses during pathogenesis. PubMed: 17719490DOI: 10.1016/j.chembiol.2007.07.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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