Lysine 114 of Antithrombin Is of Crucial Importance for the Affinity and Kinetics of Heparin Pentasaccharide Binding
Open Access
- 1 November 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (47) , 43809-43817
- https://doi.org/10.1074/jbc.m105294200
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Partitioning of Serpin-Proteinase Reactions between Stable Inhibition and Substrate Cleavage Is Regulated by the Rate of Serpin Reactive Center Loop Insertion into β-Sheet AJournal of Biological Chemistry, 2000
- Lysine Residue 114 in Human Antithrombin III Is Required for Heparin Pentasaccharide-mediated ActivationJournal of Biological Chemistry, 1997
- The 2.6 Å structure of antithrombin indicates a conformational change at the heparin binding site 1 1Edited by R. HuberJournal of Molecular Biology, 1997
- Requirement of Lysine Residues Outside of the Proposed Pentasaccharide Binding Region for High Affinity Heparin Binding and Activation of Human Antithrombin IIIPublished by Elsevier ,1996
- Lysine-Heparin Interactions in Antithrombin. Properties of K125M and K290M,K294M,K297M VariantsBiochemistry, 1994
- .alpha.1-Proteinase Inhibitor Variant T345R. Influence of P14 Residue on Substrate and Inhibitory PathwaysBiochemistry, 1994
- Carbohydrate isoforms of antithrombin variant N135Q with different heparin affinitiesFEBS Letters, 1993
- Structure-activity relationship in heparin: A synthetic pentasaccharide with high affinity for antithrombin III and eliciting high anti-factor Xa activityBiochemical and Biophysical Research Communications, 1983
- Characterization of specific receptors for vasopressin in the pituitary glandBiochemical and Biophysical Research Communications, 1983
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970