0000000000236097

AUTHOR

Mitsuru Tashiro

showing 2 related works from this author

High-resolution solution NMR structure of the Z domain of staphylococcal protein A

1997

Staphylococcal protein A (SpA) is a cell-wall-bound pathogenicity factor from the bacterium Staphylococcus aureus. Because of their small size and immunoglobulin (IgG)-binding activities, domains of protein A are targets for protein engineering efforts and for the development of computational approaches for de novo protein folding. The NMR solution structure of an engineered IgG-binding domain of SpA, the Z domain (an analog of the B domain of SpA), has been determined by simulated annealing with restrained molecular dynamics on the basis of 671 conformational constraints. The Z domain contains three well-defined alpha-helices corresponding to polypeptide segments Lys7 to Leu17 (helix 1), G…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationChemistryMolecular Sequence DataProtein engineeringHydrogen-Ion ConcentrationCrystallography X-RayAntiparallel (biochemistry)CrystallographyModels ChemicalStructural BiologyHelixHumansHydrogen–deuterium exchangeAmino Acid SequenceB3 domainStaphylococcal Protein AMolecular BiologyTwo-dimensional nuclear magnetic resonance spectroscopyConformational isomerismHeteronuclear single quantum coherence spectroscopyJournal of Molecular Biology
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The mechanism of binding staphylococcal protein A to immunoglobin G does not involve helix unwinding.

1996

Structural changes in staphylococcal protein A (SpA) upon its binding to the constant region (Fc) of immunoglobulin G (IgG) have been studied by nuclear magnetic resonance and circular dichroism (CD) spectroscopy. The NMR solution structure of the engineered IgG-binding domain of SpA, the Z domain (an analogue of the B domain of SpA), has been determined by simulated annealing with molecular dynamics, using 599 distance and dihedral angle constraints. Domain Z contains three alpha-helices in the polypeptide segments Lys7 to His18 (helix 1), Glu25 to Asp36 (helix 2), and Ser41 to Ala54 (helix 3). The overall chain fold is an antiparallel three-helical bundle. This is in contrast to the previ…

Models MolecularCircular dichroismProtein FoldingMagnetic Resonance SpectroscopyStereochemistryMolecular Sequence DataPlasma protein bindingDihedral angleBiochemistryProtein Structure SecondaryProtein structureComputer GraphicsAmino Acid SequenceBinding siteStaphylococcal Protein ABinding SitesChemistryCircular DichroismNuclear magnetic resonance spectroscopyRecombinant ProteinsImmunoglobulin Fc FragmentsModels StructuralCrystallographyIgG bindingImmunoglobulin GMutagenesis Site-DirectedProtein foldingProtein BindingBiochemistry
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