Phosphorylation Regulates the Bound Structure of an Intrinsically Disordered Protein: The p53-TAZ2 Case

Open Access

Peer-reviewed

Research Article

Raúl Esteban Ithuralde,

Affiliations Departamento de Química Inorgánica, Analítica y Química Física y Departamento de Química Biológica-Facultad de Ciencias Exacas y Naturales-Universidad de Buenos Aires, ciudad de Buenos Aires, Argentina, INQUIMAE-Facultad de Ciencias Exactas y Naturales-Universidad de Buenos Aires/Consejo Nacional de Investigaciones Científicas y Técnicas-CONICET, ciudad de Buenos Aires, Argentina
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Adrián Gustavo Turjanski

* E-mail: adrian@qi.fcen.uba.ar

Affiliations Departamento de Química Inorgánica, Analítica y Química Física y Departamento de Química Biológica-Facultad de Ciencias Exacas y Naturales-Universidad de Buenos Aires, ciudad de Buenos Aires, Argentina, INQUIMAE-Facultad de Ciencias Exactas y Naturales-Universidad de Buenos Aires/Consejo Nacional de Investigaciones Científicas y Técnicas-CONICET, ciudad de Buenos Aires, Argentina
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Phosphorylation
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Intrinsically disordered proteins
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Protein structure
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Protein interactions
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Phosphates
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Biochemical simulations
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Transcription factors
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DNA-binding proteins
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