Abstract
We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in dramatically reduced overlap, was applied to the interaction of the integrin αvβ6 with a known peptide ligand and highlights novel contact points between the substrate and target protein.
MeSH terms
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Amino Acid Sequence
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Antigens, Neoplasm / chemistry
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Antigens, Neoplasm / metabolism*
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Binding Sites
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Foot-and-Mouth Disease Virus / chemistry
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Foot-and-Mouth Disease Virus / metabolism*
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Humans
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Integrins / chemistry
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Integrins / metabolism*
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular / methods*
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Peptides / chemistry
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Peptides / metabolism*
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Protein Binding
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Receptors, Virus / chemistry
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Receptors, Virus / metabolism*
Substances
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Antigens, Neoplasm
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Integrins
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Peptides
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Receptors, Virus
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integrin alphavbeta6