Cysteine pairing in the glycoprotein IIbIIIa antagonist kistrin using NMR, chemical analysis, and structure calculations

The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet aggregation. Kistrin belongs to a family of homologous proteins found in snake venoms termed disintegrins, a...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1993-01, Vol.32 (1), p.282-289
Main Authors: ADLER, M, CARTER, P, LAZARUS, R. A, WAGNER, G
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Biological and medical sciences
Chemical Phenomena
Chemistry, Physical
Crotalid Venoms - chemistry
Cysteine - chemistry
Disulfides - chemistry
Endopeptidases - metabolism
Fundamental and applied biological sciences. Psychology
Magnetic Resonance Spectroscopy
Miscellaneous
Molecular Sequence Data
Molecular Structure
Peptide Fragments - chemistry
Peptides - chemistry
Platelet Aggregation Inhibitors - chemistry
Platelet Membrane Glycoproteins - antagonists & inhibitors
Protein Structure, Secondary
Proteins
Viper Venoms - chemistry
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The pairing of the cysteines in disulfide bonds was investigated for the 68-residue RGD-containing protein kistrin, a potent antagonist of the integrin GP IIbIIIa and an inhibitor of platelet aggregation. Kistrin belongs to a family of homologous proteins found in snake venoms termed disintegrins, all of which have a cysteine content. The disulfide pairing of the 12 cysteines was investigated by chemical analysis, NMR spectroscopy, and distance geometry calculations. The data show that the disulfide pairs are 4-19, 6-14, 13-36, 27-33, 32-57, and 45-64. The various means for assigning the disulfide bonds are described, and the results are compared with the cysteine pairings reported for other disintegrin proteins.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00052a036