1inq
Structure of Minor Histocompatibility Antigen peptide, H13a, complexed to H2-Db
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OverviewOverview
The mouse H13 minor histocompatibility (H) Ag, originally detected as a, barrier to allograft transplants, is remarkable in that rejection is a, consequence of an extremely subtle interchange, P4(Val/Ile), in a nonamer, H2-D(b)-bound peptide. Moreover, H13 peptides lack the canonical P5(Asn), central anchor residue normally considered important for forming a, peptide/MHC complex. To understand how these noncanonical peptide pMHC, complexes form physiologically active TCR ligands, crystal structures of, allelic H13 pD(b) complexes and a P5(Asn) anchored pD(b) analog were, solved to high resolution. The structures show that the basis of TCRs to, distinguish self from nonself H13 peptides is their ability to distinguish, a single solvent-exposed methyl group. In addition, the structures, demonstrate that there is no need for H13 peptides to derive any, stabilization from interactions within the central C pocket to generate, fully functional pMHC complexes. These results provide a structural, explanation for a classical non-MHC-encoded H Ag, and they call into, question the requirement for contact between anchor residues and the major, MHC binding pockets in vaccine design.
About this StructureAbout this Structure
1INQ is a Protein complex structure of sequences from Mus musculus with DMS as ligand. Full crystallographic information is available from OCA.
ReferenceReference
How H13 histocompatibility peptides differing by a single methyl group and lacking conventional MHC binding anchor motifs determine self-nonself discrimination., Ostrov DA, Roden MM, Shi W, Palmieri E, Christianson GJ, Mendoza L, Villaflor G, Tilley D, Shastri N, Grey H, Almo SC, Roopenian D, Nathenson SG, J Immunol. 2002 Jan 1;168(1):283-9. PMID:11751972
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