Crystal structures of human 17β-hydroxysteroid dehydrogenase type 1 complexed with estrone and NADP
17-Hydroxysteroid Dehydrogenases
/ chemistry
Amino Acid Sequence
/ genetics
Binding Sites
/ genetics
Catalysis
Crystallography, X-Ray
Enzyme Inhibitors
/ chemistry
Estrogens
/ chemistry
Estrone
/ chemistry
Humans
Models, Molecular
NADP
/ chemistry
Oxidation-Reduction
Protein Binding
/ genetics
Protein Conformation
Substrate Specificity
17β-HSD1
crystal structure
dead-end complex
reverse binding
substrate inhibition
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
06 2019
06 2019
Historique:
received:
05
11
2018
revised:
28
01
2019
accepted:
13
02
2019
pubmed:
16
2
2019
medline:
16
5
2020
entrez:
16
2
2019
Statut:
ppublish
Résumé
Human 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1) catalyses the last step in estrogen activation and is thus involved in estrogen-dependent diseases (EDDs). Unlike other 17β-HSD members, 17β-HSD1 undergoes a significant substrate-induced inhibition that we have previously reported. Here we solved the binary and ternary crystal structures of 17β-HSD1 in complex with estrone (E1) and cofactor analog NADP
Substances chimiques
Enzyme Inhibitors
0
Estrogens
0
Estrone
2DI9HA706A
NADP
53-59-8
17-Hydroxysteroid Dehydrogenases
EC 1.1.-
3 (or 17)-beta-hydroxysteroid dehydrogenase
EC 1.1.1.51
Banques de données
PDB
['6MNC', '6MNE', 'IIOL', '1IOL', '1JTV', '1ERE']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2155-2166Subventions
Organisme : Canadian Institutes of Health Research
Pays : International
Informations de copyright
© 2019 Federation of European Biochemical Societies.