Solution structure of kistrin, a potent platelet aggregation inhibitor and GP IIb-IIIa antagonist.
The structure of kistrin, which is a member of a homologous family of glycoprotein IIb-IIIa (GP IIb-IIIa) antagonists and potent protein inhibitors of platelet aggregation, has been determined by two-dimensional nuclear magnetic resonance (NMR) spectroscopy. The 68-residue protein consists of a series of tightly packed loops held together by six disulfide bonds and has almost no regular secondary structure. Kistrin has an Arg-Gly-Asp (RGD) adhesion site recognition sequence important for binding to GP IIb-IIIa that is located at the apex of a long loop across the surface of the protein.
Adler
M
M
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Lazarus
R A
RA
Dennis
M S
MS
Wagner
G
G
D000595:Amino Acid Sequence; D006023:Glycoproteins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010455:Peptides / Q000737:chemistry* / Q000235:genetics; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*; D010980:Platelet Membrane Glycoproteins / Q000037:antagonists & inhibitors*; D011487:Protein Conformation
D006023:Glycoproteins; D010455:Peptides; D010975:Platelet Aggregation Inhibitors; D010980:Platelet Membrane Glycoproteins; C067623:kistrin