The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection
Identifieur interne : 002602 ( Istex/Curation ); précédent : 002601; suivant : 002603The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection
Auteurs : Aideen C. M. Young [États-Unis] ; Weiguo Zhang [États-Unis] ; James C. Sacchettini [États-Unis] ; Stanley G. Nathenson [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1994.
English descriptors
- Teeft :
- Alla2, Allele, Amino, Amino acids, Anchor residue, Anchor residues, Backbone atoms, Bjorkman, Cell receptor, Chemical properties, Cleft, Cleft residues, Conformation, Corresponding positions, Cytotoxic, Different residues, Diffraction data, Direct hydrogen bonds, Evolutionary pressure, Evolutionary relationship, Falk, Fremont, Groove, Heavy chain, Heavy chains, Helix, Histocompatibility, Human class, Hydrogen bond, Hydrogen bonds, Hydrophobic, Hydrophobic residue, Hydrophobic ridge, Influenza, Influenza nucleoprotein, Influenza peptide, Influenza virus, Influenza virus peptide, Large number, Main chain, Main chain atoms, Main chain deviation, Main chain nitrogen atom, Major histocompatibility, Model building, Molecule, Molecules share, Mouse class, Murine, Murine class, Murine products, Nathenson, P3asn, P5asn, P9met, Peptide, Peptide anchor residues, Peptide antigens, Peptide backbone, Peptide binding, Peptide residue, Peptide residues, Peptide side chains, Peptide termini, Peptides bind, Prim, Prim domains, Receptor, Refined structure, Residue, Sequence identity, Side chain, Side chain atoms, Side chains, Single solution, Solvent accessibility, Solvent molecules, Strominger, Structural basis, Structural feature, Structural features, Structural subgroup, Surface area, Total surface area, Transplantation antigens, Variable residues, Vesicular stomatitis virus, Waals interactions, Water molecules, Zhang.
Abstract
Abstract: Solution at 2.4 Å resolution of the structure of H-2Db with the influenza virus peptide NP366–374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides that can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.
Url:
DOI: 10.1016/0092-8674(94)90171-6
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<term>Amino acids</term>
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<term>Anchor residues</term>
<term>Backbone atoms</term>
<term>Bjorkman</term>
<term>Cell receptor</term>
<term>Chemical properties</term>
<term>Cleft</term>
<term>Cleft residues</term>
<term>Conformation</term>
<term>Corresponding positions</term>
<term>Cytotoxic</term>
<term>Different residues</term>
<term>Diffraction data</term>
<term>Direct hydrogen bonds</term>
<term>Evolutionary pressure</term>
<term>Evolutionary relationship</term>
<term>Falk</term>
<term>Fremont</term>
<term>Groove</term>
<term>Heavy chain</term>
<term>Heavy chains</term>
<term>Helix</term>
<term>Histocompatibility</term>
<term>Human class</term>
<term>Hydrogen bond</term>
<term>Hydrogen bonds</term>
<term>Hydrophobic</term>
<term>Hydrophobic residue</term>
<term>Hydrophobic ridge</term>
<term>Influenza</term>
<term>Influenza nucleoprotein</term>
<term>Influenza peptide</term>
<term>Influenza virus</term>
<term>Influenza virus peptide</term>
<term>Large number</term>
<term>Main chain</term>
<term>Main chain atoms</term>
<term>Main chain deviation</term>
<term>Main chain nitrogen atom</term>
<term>Major histocompatibility</term>
<term>Model building</term>
<term>Molecule</term>
<term>Molecules share</term>
<term>Mouse class</term>
<term>Murine</term>
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<term>Murine products</term>
<term>Nathenson</term>
<term>P3asn</term>
<term>P5asn</term>
<term>P9met</term>
<term>Peptide</term>
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<term>Peptide antigens</term>
<term>Peptide backbone</term>
<term>Peptide binding</term>
<term>Peptide residue</term>
<term>Peptide residues</term>
<term>Peptide side chains</term>
<term>Peptide termini</term>
<term>Peptides bind</term>
<term>Prim</term>
<term>Prim domains</term>
<term>Receptor</term>
<term>Refined structure</term>
<term>Residue</term>
<term>Sequence identity</term>
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<term>Side chains</term>
<term>Single solution</term>
<term>Solvent accessibility</term>
<term>Solvent molecules</term>
<term>Strominger</term>
<term>Structural basis</term>
<term>Structural feature</term>
<term>Structural features</term>
<term>Structural subgroup</term>
<term>Surface area</term>
<term>Total surface area</term>
<term>Transplantation antigens</term>
<term>Variable residues</term>
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<front><div type="abstract" xml:lang="en">Abstract: Solution at 2.4 Å resolution of the structure of H-2Db with the influenza virus peptide NP366–374 (ASNEN-METM) and comparison with the H-2Kb-VSV (RGY-VYQGL) structure allow description of the molecular details of MHC class I peptide binding interactions for mice of the H-2b haplotype, revealing a strategy that maximizes the repertoire of peptides that can be presented. The H-2Db cleft has a mouse-specific hydrophobic ridge that causes a compensatory arch in the backbone of the peptide, exposing the arch residues to TCR contact and requiring the peptide to be at least 9 residues. This ridge occurs in about 40% of the known murine D and L allelic molecules, classifying them as a structural subgroup.</div>
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