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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.","bibjson":{"author":[{"initials":"C","lastname":"Ciatto","name":"Ciatto C"},{"initials":"AC","lastname":"Tissot","name":"Tissot AC"},{"initials":"M","lastname":"Tschopp","name":"Tschopp M"},{"initials":"G","lastname":"Capitani","name":"Capitani G"},{"initials":"F","lastname":"Pecorari","name":"Pecorari F"},{"initials":"A","lastname":"Pl\u00fcckthun","name":"Pl\u00fcckthun A"},{"initials":"MG","lastname":"Gr\u00fctter","name":"Gr\u00fctter MG"}],"identifier":[{"id":"10.1006/jmbi.2001.5016","type":"doi"},{"id":"11580250","type":"pubmed"}],"issue":["5"],"journal":{"iso_abbreviation":"J. Mol. 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