Insights into the induced fit mechanism in antithrombin–heparin interaction using molecular dynamics simulations

• Published in: Journal of molecular graphics & modelling Vol. 24; no. 3; pp. 203 - 212
• Main Authors: Verli, Hugo, Guimarães, Jorge A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.12.2005
• Subjects: Allosteric Regulation; Allosteric Site; Amino Acid Sequence; Amino Acids - chemistry; Amino Acids - metabolism; Antithrombin; Antithrombins - chemistry; Antithrombins - metabolism; Carbohydrate; Carbohydrate Sequence; Computer Simulation; Drug Design; Fibrinolytic Agents - chemistry; Heparin; Heparin - chemistry; Heparin - metabolism; Induced fit; Ligands; Models, Chemical; Molecular dynamics; Molecular Sequence Data; Oligosaccharides - chemistry; Oligosaccharides - metabolism; Protein Conformation; Serpin; Synthetic pentasaccharide; Time Factors; Serpin; Induced fit; Molecular dynamics; Carbohydrate; Synthetic pentasaccharide; Heparin; Antithrombin

Heparin was isolated in the beginning of the 20th century and until today remains as one of the most important drugs able to interfere with the haemostatic process. Due to the side effects produced by heparin therapy, new promising drugs have been developed, as the synthetic pentasaccharide (synthet...