1H NMR studies of echistatin in solution. Sequential resonance assignments and secondary structure.

摘要: Two-dimensional 1H-NMR methods have been used to obtain complete proton resonance assignments for the 49-residue protein echistatin from viper Echis carinatus. The in solution contains only a small amount of regular secondary structure with four very short β-strands. These β-strands form two segments antiparallel β-sheet, as evidenced by observed cross-strand NOE. first strands are connected tight reverse turn, whereas remaining linked together an 11-residue loop forming so-called hairpin. tripeptide unit Arg-Gly-Asp, responsible binding fibrinogen receptor glycoprotein GPIIb/IIIa, is located at tip this hydrophilic loop.