1S7S

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

Summary for 1S7S

• Entry DOI: 10.2210/pdb1s7s/pdb
• Related: 1n59 1s7q 1s7r 1s7t 1s7u 1s7v 1s7w 1s7x
• Descriptor: H-2 class I histocompatibility antigen, K-B alpha chain, Beta-2-microglobulin, Glycoprotein 9-residue peptide, ... (4 entities in total)
• Functional Keywords: lcmv, mhc class i, immune escape, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01901; Secreted: P01887; Stable signal peptide: Virion membrane; Multi-pass membrane protein (Potential). Glycoprotein G1: Virion membrane; Peripheral membrane protein (Potential). Glycoprotein G2: Virion membrane; Single- pass membrane protein (Potential): P07399
• Total number of polymer chains: 3
• Total formula weight: 51963.67

Authors

Velloso, L.M.,Michaelsson, J.,Ljunggren, H.G.,Schneider, G.,Achour, A. (deposition date: 2004-01-30, release date: 2004-05-04, Last modification date: 2023-08-23)

Primary citation

Velloso, L.M.,Michaelsson, J.,Ljunggren, H.G.,Schneider, G.,Achour, A.
Determination of structural principles underlying three different modes of lymphocytic choriomeningitis virus escape from CTL recognition.
J.Immunol., 172:5504-5511, 2004

PubMed Abstract: 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.

PubMed: 15100292

Experimental method

X-RAY DIFFRACTION (1.99 Å)