The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
Identifieur interne : 004742 ( Main/Exploration ); précédent : 004741; suivant : 004743The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
Auteurs : Dean R. Madden [États-Unis] ; Joan C. Gorga [États-Unis] ; Jack L. Strominger [États-Unis] ; Don C. Wiley [États-Unis]Source :
- Cell [ 0092-8674 ] ; 1992.
English descriptors
- Teeft :
- Acta, Acta cryst, Additional water molecules, Amino acids, Ankylosing spondylitis, Arginine, Arginine guanidinium group, Arginine side chain, Asymmetric unit, Binding cleft, Binding interactions, Binding site, Biol, Bjorkman, Carbonyl oxygen, Cell surface, Chains, Cleft, Concave surface, Conformation, Cryst, Crystal contact, Crystal structures, Disease association, Electron density, Electron density maps, Gorga, Harvest buffer, Heavy chain, Helix, Histocompatibility, Histocompatibility antigens, Hydrogen bond, Hydrogen bonds, Immunol, Jardetzky, Main chain, Major histocompatibility, Model building, Molecule, Other class, Parham, Peptide, Peptide atoms, Peptide binding, Peptide electron density, Peptide model, Peptide population, Peptide residues, Peptide side chains, Peptide termini, Program hydraster, Refinement, Residue, Room temperature, Rrikaitlk, Saper, Sequence variability, Side chain, Side chains, Sodium azide, Strominger, Structure factor amplitudes, Subtypes, Surface area, Terminus, Tight peptide binding, Townsend, Unpublished data, Water molecule, Water molecules.
Abstract
Abstract: Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
Url:
DOI: 10.1016/0092-8674(92)90252-8
Affiliations:
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The 2.1 Å structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a cocrystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an “anchor” side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Massachusetts</li><li>Pennsylvanie</li></region></list><tree><country name="États-Unis"><region name="Massachusetts"><name sortKey="Madden, Dean R" sort="Madden, Dean R" uniqKey="Madden D" first="Dean R." last="Madden">Dean R. Madden</name></region><name sortKey="Gorga, Joan C" sort="Gorga, Joan C" uniqKey="Gorga J" first="Joan C." last="Gorga">Joan C. Gorga</name><name sortKey="Gorga, Joan C" sort="Gorga, Joan C" uniqKey="Gorga J" first="Joan C." last="Gorga">Joan C. Gorga</name><name sortKey="Madden, Dean R" sort="Madden, Dean R" uniqKey="Madden D" first="Dean R." last="Madden">Dean R. 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