PuSH - Publication Server of Helmholtz Zentrum München: New insights into human 17β-hydroxysteroid dehydrogenase type 14: First crystal structures in complex with a steroidal ligand and with a potent non-steroidal inhibitor.

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Bertoletti, N.* ; Braun, F.* ; Lepage, M.* ; Möller, G. ; Adamski, J. ; Heine, A.* ; Klebe, G.* ; Marchais-Oberwinkler, S.*

New insights into human 17β-hydroxysteroid dehydrogenase type 14: First crystal structures in complex with a steroidal ligand and with a potent non-steroidal inhibitor.

J. Med. Chem. 59, 6961-6967 (2016)

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17β-HSD14 is a SDR enzyme, able to oxidize estradiol and 5-androstenediol using NAD(+). We determined the crystal structure of this human enzyme as the holo form and as ternary complexes with estrone and with the first potent, non-steroidal inhibitor. The structures reveal a conical, rather large and lipophilic binding site and are the starting point for structure-based inhibitor design. The two natural variants (S205 and T205) were characterized and adopt a similar structure.

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Publication type Article: Journal article

Document type Scientific Article

Corresponding Author

ISSN (print) / ISBN 0022-2623

e-ISSN 1520-4804

Journal Journal of Medicinal Chemistry

Quellenangaben Volume: 59, Issue: 14, Pages: 6961-6967

Publisher American Chemical Society (ACS)

Non-patent literature Publications

Reviewing status Peer reviewed

Institute(s) Molekulare Endokrinologie und Metabolismus (MEM)