Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions.
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.
Wagstaff
Jane L
JL
Protein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK.
Vallath
Sabari
S
Marshall
John F
JF
Williamson
Richard A
RA
Howard
Mark J
MJ
D000595:Amino Acid Sequence; D000951:Antigens, Neoplasm / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D029544:Foot-and-Mouth Disease Virus / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011991:Receptors, Virus / Q000737:chemistry / Q000378:metabolism*
D000951:Antigens, Neoplasm; D016023:Integrins; D010455:Peptides; D011991:Receptors, Virus; C073878:integrin alphavbeta6