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Biochemical Reconstitution of Steroid Receptor•Hsp90 Protein Complexes and Reactivation of Ligand Binding

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Published on: September 21, 2011

Substrate binding process and mechanistic functioning of type 1 11β-hydroxysteroid dehydrogenase from enhanced

Angelo D Favia¹, Matteo Masetti, Maurizio Recanatini

¹Drug Discovery and Development Department, Istituto Italiano di Tecnologia, Genoa, Italy. angelo.favia@iit.it

|October 4, 2011

Summary

Type 1 11β-hydroxysteroid dehydrogenase (11β-HSD-1) dynamic behavior was simulated upon substrate binding. This study reveals key insights into enzyme-substrate interactions, dimerisation, and ligand recognition.

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Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry

Published on: November 29, 2013

Area of Science:

Biochemistry
Molecular Biology
Structural Biology

Background:

Type 1 11β-hydroxysteroid dehydrogenase (11β-HSD-1) regulates glucocorticoid balance by converting cortisone to cortisol.
X-ray structures and experimental data have elucidated many functional aspects of 11β-HSD-1.
A comprehensive understanding of 11β-HSD-1's dynamic behavior during substrate binding is currently lacking.

Purpose of the Study:

To investigate the dynamic behavior of 11β-HSD-1 during substrate binding using computational methods.
To elucidate the molecular mechanisms underlying the enzyme-substrate relationship for 11β-HSD-1.
To provide a detailed description of 11β-HSD-1's dynamic interactions with its natural substrate, cortisone.

Main Methods:

Molecular docking of cortisone into the catalytic site of wild-type and Y177A mutant 11β-HSD-1.
Steered molecular dynamics and metadynamics simulations to model cortisone undocking from 11β-HSD-1.
Computational analysis of enzyme-substrate interactions at a molecular level.

Main Results:

The study identified the molecular basis for the functional dimerisation of 11β-HSD-1.
The critical role of the Y177 residue in the cortisone binding event was highlighted.
Key insights were gained into the regulation of active site solvation and the function of the S228-P237 loop in ligand recognition.

Conclusions:

The computational simulations provide a detailed molecular-level understanding of 11β-HSD-1's dynamic response to substrate binding.
The findings clarify the structural and dynamic determinants of 11β-HSD-1 activity and substrate interaction.
This work enhances our knowledge of glucocorticoid metabolism regulation by 11β-HSD-1.