2qri
Crystal structure of a single chain trimer composed of the MHC I heavy chain H-2Kb WT, beta-2microglobulin, and ovalbumin-derived peptide.
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | H2-K1, H2-K, B2m (Mus musculus) | ||||||
| Related: | 2QRS, 2QRT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
2QRI is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Structural engineering of pMHC reagents for T cell vaccines and diagnostics., Mitaksov V, Truscott SM, Lybarger L, Connolly JM, Hansen TH, Fremont DH, Chem Biol. 2007 Aug;14(8):909-22. PMID:17719490
Page seeded by OCA on Mon Mar 31 04:52:36 2008