1H NMR studies of echistatin in solution. Sequential resonance assignments and secondary structure.
Two-dimensional 1H-NMR methods have been used to obtain complete proton resonance assignments for the 49-residue protein echistatin from the viper Echis carinatus. The protein in solution contains only a small amount of regular secondary structure with four very short beta-strands. These beta-strands form two short segments of antiparallel beta-sheet, as evidenced by the observed cross-strand NOE. The first two strands are connected with a tight reverse turn, whereas the remaining two strands are linked together by an 11-residue loop forming a so-called hairpin. The tripeptide unit Arg-Gly-Asp, responsible for the binding of echistatin to the fibrinogen receptor glycoprotein GPIIb/IIIa, is located at the tip of this very hydrophilic loop.
Dalvit
C
C
Preclinical Research, Sandoz Pharma AG.
Widmer
H
H
Bovermann
G
G
Breckenridge
R
R
Metternich
R
R
D000595:Amino Acid Sequence; D004220:Disulfides / Q000737:chemistry; D036341:Intercellular Signaling Peptides and Proteins; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010455:Peptides; D010980:Platelet Membrane Glycoproteins / Q000378:metabolism; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012996:Solutions; D014757:Viper Venoms / Q000737:chemistry* / Q000378:metabolism
D004220:Disulfides; D036341:Intercellular Signaling Peptides and Proteins; D009842:Oligopeptides; D010455:Peptides; D010980:Platelet Membrane Glycoproteins; D012996:Solutions; D014757:Viper Venoms; C057986:echistatin; C047981:arginyl-glycyl-aspartic acid