• Home
  • Search Results
  • Site-directed mutagenesis to study the role of specific amino acids in the ligand binding domain of PPARs.

Site-directed mutagenesis to study the role of specific amino acids in the ligand binding domain of PPARs.

Methods in molecular biology (Clifton, N.J.) (2012-10-27)
Nico Mitro, Federica Gilardi, Marco Giudici, Cristina Godio, Elena Scotti, Maurizio Crestani
ABSTRACT

The role of certain amino acids in the interactions of ligands with their cognate nuclear receptors is usually achieved by the resolution of the crystal structure of the receptor complexed with the ligand. As a complementary functional approach, site-directed mutagenesis, a technique broadly used in molecular biology, allows the assessment of the role of a specific amino acid in determining the interaction with a specific ligand. This method makes it possible to evaluate several mutations of a key amino acid for ligand binding and to determine the relationship between protein structure and ligand interaction. Here, we describe an application of this technique to evaluate different point mutations on the transcriptional activity of peroxisome proliferator-activated receptor γ (PPARγ) in the absence or presence of chemically different ligands.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Nde I from Neisseria denitrificans, Restriction Enzyme
Sigma-Aldrich
EclX I from Enterobacter cloacae 590, Restriction Enzyme

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.