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Related Experiment Videos

Human type 10 17 beta-hydroxysteroid dehydrogenase: molecular modelling and substrate docking.

E Nordling1, U C Oppermann, H Jörnvall

  • 1Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden.

Journal of Molecular Graphics & Modelling
|September 13, 2001
PubMed
Summary

Human 17 beta-hydroxysteroid dehydrogenase type 10 (17 beta-HSD-10) is a mitochondrial enzyme that modifies steroid hormones. Its structure was modeled to understand its role in neurodegenerative diseases and cancer.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Enzymology
  • Structural Biology

Background:

  • 17 beta-hydroxysteroid dehydrogenases (17 beta-HSDs) regulate steroid hormone activity by catalyzing C17 oxidoreduction.
  • Human 17 beta-HSD-10 is a mitochondrial enzyme with multiple functions, including steroid inactivation and fatty acid beta-oxidation.
  • Dysregulation of 17 beta-HSD-10 is implicated in neurodegenerative diseases and steroid-dependent cancers.

Purpose of the Study:

  • To elucidate the molecular basis of 17 beta-HSD-10's substrate specificities.
  • To understand the structural features of 17 beta-HSD-10 relevant to its biological functions.
  • To provide a foundation for developing novel therapeutic strategies targeting 17 beta-HSD-10.

Main Methods:

  • Homology modeling was employed to generate a three-dimensional structure of human 17 beta-HSD-10.

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  • Analysis of the predicted structure focused on active site characteristics and substrate binding cleft.
  • The model was evaluated for its ability to explain substrate specificities towards various steroid hormones.

    • Main Results:

    • The homology model revealed 17 beta-HSD-10 as a one-domain, alpha/beta fold enzyme belonging to the SDR family.
    • A large, hydrophobic cleft was identified as the active site, accommodating diverse steroid substrates.
    • The structural model provides insights into the enzyme's promiscuous substrate binding and catalytic activities.

    Conclusions:

    • The generated structural model of 17 beta-HSD-10 explains its substrate specificities for androgens and estrogens.
    • This model serves as a valuable tool for exploring substrate and inhibitor interactions.
    • The findings support the development of targeted therapeutics for neurodegenerative and malignant diseases involving 17 beta-HSD-10.