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Structural studies of the three isotypes of the peroxisomal proliferator-activated receptor hPPAR and them interaction with retinoid receptor hRXRalfa using small angle X-ray scattering

Grant number: 08/05637-9
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): October 01, 2008
Effective date (End): September 30, 2010
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:Igor Polikarpov
Grantee:Mario de Oliveira Neto
Home Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil
Associated research grant:06/00182-8 - Structural biophysics of nuclear receptors and related proteins, AP.TEM

Abstract

Nuclear receptors are of paramount importance to the processes of intercellular signaling in eukaryotes, since they have the ability to converge various internal and external signals important for the regulation of genetic programs involved in all aspects of the multicellular organism's life, such as: embryogenesis, homeostasis, reproduction, growth and cell death. The transcriptional regulation and selectivity promoted by these proteins have fostered intense research with the objective to unveil the complex network of molecular events that describe their way of action. Now a day, the full knowledge of the rules that promote the spatial and temporal control of gene expression by the nuclear receptors is still an important challenge. In this context, we propose as the main objective of this project to carry out SAXS studies of the interactions of the three isotypes of the Peroxisome Proliferator-Activated Receptor (PPAR) with isoform alfa of the 9-cis Retinoic Acid Receptor (hRXRalfa). Different constructs of PPAR isotypes and RXR will be analyzed, such as: the full-length protein, constructs containing both DNA binding domain (DBD) and ligand binding domain (LBD), and constructs with only the ligand binding domain (LBD). We hope that the results will enable us to determine the spatial position of the different domains present in the full-length nuclear receptors; as well as, to verify conformational changes, if they exist, when proteins are exposed to their ligands, cofactors, responsive elements, or to other elements of the superfamily. (AU)

Scientific publications
(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)
SEGATO, FERNANDO; BERTO, GABRIELA L.; DE ARAUJO, EVANDRO ARES; MUNIZ, JOAO RENATO; POLIKARPOV, IGOR. Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-beta-1,4-glucanase from glycoside hydrolase family 12. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v. 70, n. 2, p. 267-270, FEB 2014. Web of Science Citations: 3.
LIMA, LEONARDO H. F.; SERPA, VIVIANE I.; ROSSETO, FLAVIO R.; SARTORI, GERALDO RODRIGUES; DE OLIVEIRA NETO, MARIO; MARTINEZ, LEANDRO; POLIKARPOV, IGOR. Small-angle X-ray scattering and structural modeling of full-length: cellobiohydrolase I from Trichoderma harzianum. Cellulose, v. 20, n. 4, p. 1573-1585, AUG 2013. Web of Science Citations: 7.
BERNARDES, AMANDA; BATISTA, FERNANDA A. H.; NETO, MARIO DE OLIVEIRA; FIGUEIRA, ANA CAROLINA M.; WEBB, PAUL; SAIDEMBERG, DANIEL; PALMA, MARIO S.; POLIKARPOV, IGOR. Low-Resolution Molecular Models Reveal the Oligomeric State of the PPAR and the Conformational Organization of Its Domains in Solution. PLoS One, v. 7, n. 2 FEB 21 2012. Web of Science Citations: 12.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.