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Int. J. Mol. Sci. 2017, 18(2), 361;

Single-Nucleotide Polymorphism of PPARγ, a Protein at the Crossroads of Physiological and Pathological Processes

Department of Biochemical Sciences “A. Rossi Fanelli”, Sapienza University of Rome, P.le A. Moro, 5, 00185 Rome, Italy
SSPT-BIOAG-BIOTEC ENEA Casaccia ENEA, 00123 Rome, Italy
Department of Physics, University of Rome Tor Vergata and INFN, Via della Ricerca Scientifica 1, 00133 Roma, Italy
Dipartimento di Farmacia-Scienze del Farmaco, University of Bari, 70126 Bari, Italy
Istituto di Cristallografia, Consiglio Nazionale delle Ricerche, Via Salaria Km. 29, 300, Monterotondo Stazione, 00015 Roma, Italy
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editors: Emil Alexov and Stephen A. Bustin
Received: 31 October 2016 / Revised: 24 January 2017 / Accepted: 1 February 2017 / Published: 10 February 2017
(This article belongs to the Collection Human Single Nucleotide Polymorphisms and Disease Diagnostics)
Full-Text   |   PDF [2192 KB, uploaded 17 February 2017]   |  


Genome polymorphisms are responsible for phenotypic differences between humans and for individual susceptibility to genetic diseases and therapeutic responses. Non-synonymous single-nucleotide polymorphisms (nsSNPs) lead to protein variants with a change in the amino acid sequence that may affect the structure and/or function of the protein and may be utilized as efficient structural and functional markers of association to complex diseases. This study is focused on nsSNP variants of the ligand binding domain of PPARγ a nuclear receptor in the superfamily of ligand inducible transcription factors that play an important role in regulating lipid metabolism and in several processes ranging from cellular differentiation and development to carcinogenesis. Here we selected nine nsSNPs variants of the PPARγ ligand binding domain, V290M, R357A, R397C, F360L, P467L, Q286P, R288H, E324K, and E460K, expressed in cancer tissues and/or associated with partial lipodystrophy and insulin resistance. The effects of a single amino acid change on the thermodynamic stability of PPARγ, its spectral properties, and molecular dynamics have been investigated. The nsSNPs PPARγ variants show alteration of dynamics and tertiary contacts that impair the correct reciprocal positioning of helices 3 and 12, crucially important for PPARγ functioning. View Full-Text
Keywords: PPARγ; molecular dynamics; protein stability; single-nucleotide polymorphism PPARγ; molecular dynamics; protein stability; single-nucleotide polymorphism

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Petrosino, M.; Lori, L.; Pasquo, A.; Lori, C.; Consalvi, V.; Minicozzi, V.; Morante, S.; Laghezza, A.; Giorgi, A.; Capelli, D.; Chiaraluce, R. Single-Nucleotide Polymorphism of PPARγ, a Protein at the Crossroads of Physiological and Pathological Processes. Int. J. Mol. Sci. 2017, 18, 361.

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