1s7q
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Crystal structures of the murine class I major histocompatibility complex H-2Kb in complex with LCMV-derived gp33 index peptide and three of its escape variants
OverviewOverview
Lymphocytic choriomeningitis virus infection of H-2(b) mice generates a, strong CD8(+) CTL response mainly directed toward three immunodominant, epitopes, one of which, gp33, is presented by both H-2D(b) and H-2K(b) MHC, class I molecules. This CTL response acts as a selective agent for the, emergence of viral escape variants. These variants generate altered, peptide ligands (APLs) that, when presented by class I MHC molecules, antagonize CTL recognition and ultimately allow the virus to evade the, cellular immune response. The emergence of APLs of the gp33 epitope is, particularly advantageous for LCMV, as it allows viral escape in the, context of both H-2D(b) and H-2K(b) MHC class I molecules. We have, determined crystal structures of three different APLs of gp33 in complex, with both H-2D(b) and H-2K(b). Comparison between these APL/MHC structures, and those of the index gp33 peptide/MHC reveals the structural basis for, three different strategies used by LCMV viral escape mutations: 1), conformational changes in peptide and MHC residues that are potential TCR, contacts, 2) impairment of APL binding to the MHC peptide binding cleft, and 3) introduction of subtle changes at the TCR/pMHC interface, such as, the removal of a single hydroxyl group.
About this StructureAbout this Structure
1S7Q is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition., Velloso LM, Michaelsson J, Ljunggren HG, Schneider G, Achour A, J Immunol. 2004 May 1;172(9):5504-11. PMID:15100292
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