Identification of the functional states of human vitamin K epoxide reductase from molecular dynamics simulations-Reference-Cited by-同舟云学术

Identification of the functional states of human vitamin K epoxide reductase from molecular dynamics simulations

Published:2017 Issue:82 Volume:7 Page:52071-52090
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Chatron N.¹²³⁴⁵,Chalmond B.¹²³⁴⁵,Trouvé A.¹²³⁴⁵,Benoît E.⁶⁷⁸⁹,Caruel H.¹⁰¹¹⁹,Lattard V.⁶⁷⁸⁹,Tchertanov L.¹²³⁴⁵^ORCID

Affiliation:

1. Centre de Mathématiques et de Leurs Applications (CMLA)

2. ENS Cachan

3. CNRS

4. Université Paris-Saclay

5. Cachan

6. USC 1233 INRA-Vetagro Sup

7. Veterinary School of Lyon

8. Marcy l'Etoile

9. France

10. Liphatech

11. 47480 Pont du Casse

Abstract

The functionally-related states of hVKORC1 predicted from MD conformations were assigned by probing their affinity to vitamin K and validated through analysis of its binding energy with VKAs.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA07463H

Reference77 articles.

1. The Conversion of Vitamin K Epoxide to Vitamin K Quinone and Vitamin K Quinone to Vitamin K Hydroquinone Uses the Same Active Site Cysteines

2. VKORC1: A Warfarin‐Sensitive Enzyme in Vitamin K Metabolism and Biosynthesis of Vitamin K‐Dependent Blood Coagulation Factors

3. Vitamin K Dependent Modifications of Glutamic Acid Residues in Prothrombin

4. The realm of vitamin K dependent proteins: Shifting from coagulation toward calcification

5. The contribution of bone to whole-organism physiology

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