2QRI: Crystal Structure Of A Single Chain Trimer Composed Of The Mhc I Heavy Chain H-2kb Wt, Beta-2microglobulin, And Ovalbumin-derived Peptide

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.
PDB ID: 2QRIDownload
MMDB ID: 60569
PDB Deposition Date: 2007/7/28
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2QRI: monomeric; determined by author and by software (PISA)
Molecular Components in 2QRI
Label Count Molecule
Protein (1 molecule)
H-2 Class I Histocompatibility Antigen K-B Alpha Chain, Beta-2 Microglobulin, Ovalbumin-derived Peptide(Gene symbol: H2-K1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB