1JPG

Crystal Structure Of The LCMV Peptidic Epitope Np396 In Complex With The Murine Class I Mhc Molecule H-2Db

Summary for 1JPG

• Entry DOI: 10.2210/pdb1jpg/pdb
• Related: 1FG2 1JPF
• Descriptor: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, D-B ALPHA CHAIN, BETA-2-MICROGLOBULIN, LCMV peptidic epitope np396, ... (4 entities in total)
• Functional Keywords: ig fold, immune system
• Biological source: Mus musculus (house mouse); More
• Cellular location: Membrane; Single-pass type I membrane protein: P01899; Secreted: P01887
• Total number of polymer chains: 3
• Total formula weight: 45515.03

Authors

Ciatto, C.,Tissot, A.C.,Tschopp, M.,Capitani, G.,Pecorari, F.,Pluckthun, A.,Grutter, M.G. (deposition date: 2001-08-02, release date: 2001-10-24, Last modification date: 2024-10-30)

Primary citation

Ciatto, C.,Tissot, A.C.,Tschopp, M.,Capitani, G.,Pecorari, F.,Pluckthun, A.,Grutter, M.G.
Zooming in on the hydrophobic ridge of H-2D(b): implications for the conformational variability of bound peptides.
J.Mol.Biol., 312:1059-1071, 2001

PubMed Abstract: Class I major histocompatibility complex (MHC) molecules, which display intracellularly processed peptides on the cell surface for scanning by T-cell receptors (TCRs), are extraordinarily polymorphic. MHC polymorphism is believed to result from natural selection, since individuals heterozygous at the corresponding loci can cope with a larger number of pathogens. Here, we present the crystal structures of the murine MHC molecule H-2D(b) in complex with the peptides gp276 and np396 from the lymphocytic choriomeningitis virus (LCMV), solved at 2.18 A and 2.20 A resolution, respectively. The most prominent feature of H-2D(b) is a hydrophobic ridge that cuts across its antigen-binding site, which is conserved in the L(d)-like family of class I MHC molecules. The comparison with previously solved crystal structures of peptide/H-2D(b) complexes shows that the hydrophobic ridge focuses the conformational variability of the bound peptides in a "hot-spot", which could allow optimal TCR interaction and discrimination. This finding suggests a functional reason for the conservation of this structural element.

PubMed: 11580250
DOI: 10.1006/jmbi.2001.5016

Experimental method

X-RAY DIFFRACTION (2.2 Å)