Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods

Investigation of the Differences in Antithrombin to Heparin Binding among Antithrombin Budapest 3, Basel, and Padua Mutations by Biochemical and In Silico Methods

Antithrombin (AT) is a serine protease inhibitor, its activity is highly accelerated by heparin. Mutations at the heparin-binding region lead to functional defect, type II heparin-binding site (IIHBS) AT deficiency. The aim of this study was to investigate and compare the molecular background of AT...

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Bibliographic Details
Main Authors: Réka Gindele, Krisztina Pénzes-Daku, Gábor Balogh, Judit Kállai, Réka Bogáti, Bálint Bécsi, Ferenc Erdődi, Éva Katona, Zsuzsanna Bereczky
Format: Article
Language:English
Published: MDPI AG 2021-04-01
Series:Biomolecules
Subjects:
antithrombin
heparin-binding site
Antithrombin Budapest 3
Antithrombin Basel
Antithrombin Padua
surface plasmon resonance
Online Access:https://www.mdpi.com/2218-273X/11/4/544

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https://www.mdpi.com/2218-273X/11/4/544

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