2qrs
|
Crystal Structure of a single chain trimer composed of the MHC I heavy chain H-2Kb Y84A, beta-2microglobulin, and ovalbumin-derived peptide.
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
2QRS 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 Wed Jan 23 12:23:47 2008