X-ray structure of human aldo–keto reductase 1C3 in complex with a bile acid fused tetrazole inhibitor: experimental validation, molecular docking and structural analysis-Reference-Cited by-同舟云学术

X-ray structure of human aldo–keto reductase 1C3 in complex with a bile acid fused tetrazole inhibitor: experimental validation, molecular docking and structural analysis

Published:2023 Issue:2 Volume:14 Page:341-355
ISSN:2632-8682
Container-title:RSC Medicinal Chemistry
language:en
Short-container-title:RSC Med. Chem.

Author:

Marinović Maja A.¹,Bekić Sofija S.²,Kugler Michael³,Brynda Jiří³,Škerlová Jana³^ORCID,Škorić Dušan Đ.²^ORCID,Řezáčová Pavlína³,Petri Edward T.¹^ORCID,Ćelić Andjelka S.¹^ORCID

Affiliation:

1. Faculty of Sciences, Department of Biology and Ecology, University of Novi Sad, Trg Dositeja Obradovića 2, 21000 Novi Sad, Serbia

2. Faculty of Sciences, Department of Chemistry, Biochemistry and Environmental Protection, University of Novi Sad, Trg Dositeja Obradovića 3, 21000 Novi Sad, Serbia

3. Institute of Organic Chemistry and Biochemistry, The Czech Academy of Sciences, Flemingovo nám. 2, Prague, 16610, Czech Republic

Abstract

Steroid bile acid fused tetrazoles were screened for ability to inhibit aldo–keto reductase 1C3 (AKR1C3), a target for cancer treatment. The X-ray structure of AKR1C3 in complex with a bile acid tetrazole inhibitor is presented.

Funder

Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja

Provincial Secretariat for Higher Education and Scientific Research, Autonomous Province of Vojvodina

European Commission

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Pharmaceutical Science,Pharmacology,Molecular Medicine,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2023/MD/D2MD00387B

Reference62 articles.

1. AKR1C3 (type 5 17β-hydroxysteroid dehydrogenase/prostaglandin F synthase): Roles in malignancy and endocrine disorders