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Dissection of Hippocampal Dentate Gyrus from Adult Mouse

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Published on: November 17, 2009

Structural dataset for the PPARγ V290M mutant.

Ana C Puhl¹, Paul Webb², Igor Polikarpov¹

¹Instituto de Física de São Carlos, Universidade de São Paulo, Av. Trabalhador Saocarlense 400, São Carlos, SP 13560-970, Brazil.

|October 21, 2016

Summary

This summary is machine-generated.

A V290M mutation in peroxisome proliferator activated receptor gamma (PPARγ) causes ligand resistance syndrome. Structural data reveal how this mutation affects drug binding and receptor function, explaining clinical observations.

Keywords:

Nuclear receptors Peroxisome proliferator activated receptor γ X-ray structureç ligand resistance syndrome

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Area of Science:

Biochemistry
Structural Biology
Genetics

Background:

Loss-of-function mutation V290M in peroxisome proliferator activated receptor gamma (PPARγ) is linked to ligand resistance syndrome (PLRS).
PLRS presents with partial lipodystrophy and severe insulin resistance.

Purpose of the Study:

To present the X-ray diffraction dataset and 3D structural model of the PPARγ LBD V290M mutant.
To elucidate the molecular basis of PLRS associated with the V290M mutation.

Main Methods:

X-ray diffraction data collection and structure refinement at 2.3 Å resolution.
3D model building of the PPARγ V290M mutant.

Main Results:

A high-confidence 3D model of the PPARγ V290M mutant was generated.
Continuous electron density revealed diclofenac bound to the PPARγ hydrophobic pocket.
Structural data correlate V290M mutation with impaired rosiglitazone binding and increased corepressor affinity.

Conclusions:

The structural data provide molecular insights into the pathogenesis of PLRS caused by the V290M mutation.
The findings explain the clinical observation of treatment failure with full PPARγ agonists like rosiglitazone.