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2QRT

Crystal Structure of a disulfide trapped single chain trimer composed of the MHC I heavy chain H-2Kb Y84C, beta-2microglobulin, and ovalbumin-derived peptide.

Summary for 2QRT
Entry DOI10.2210/pdb2qrt/pdb
Related2QRI 2QRS
DescriptorH-2 class I histocompatibility antigen K-B alpha chain, Beta-2 microglobulin, ovalbumin-derived peptide (2 entities in total)
Functional Keywordsmhc-i, ova, single chain mhc-i, glycoprotein, immune response, membrane, mhc i, transmembrane, immune system
Biological sourceMus musculus (house mouse)
More
Total number of polymer chains2
Total formula weight94104.86
Authors
Mitaksov, V.E.,Fremont, D.H. (deposition date: 2007-07-29, release date: 2007-11-06, Last modification date: 2024-11-20)
Primary citationMitaksov, 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: 17719490
DOI: 10.1016/j.chembiol.2007.07.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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