The abscisic acid receptor PYR1 in complex with abscisic acid

Julia Santiago, Florine Dupeux, Adam Round, Regina Antoni, Sang-Youl Park, Marc Jamin, Sean R. Cutler, Pedro Luis Rodriguez and José Antonio Márquez ()
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Julia Santiago: Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia
Florine Dupeux: European Molecular Biology Laboratory, Grenoble Outstation and Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France
Adam Round: European Molecular Biology Laboratory, Grenoble Outstation and Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France
Regina Antoni: Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia
Sang-Youl Park: Riverside, California 92521, USA
Marc Jamin: Virus Host Cell Interactions (UVHCI) UMI 3265, Université Joseph Fourier-EMBL-CNRS, 6 rue Jules Horowitz, 38042 Grenoble Cedex 9, France
Sean R. Cutler: Riverside, California 92521, USA
Pedro Luis Rodriguez: Instituto de Biología Molecular y Celular de Plantas, Consejo Superior de Investigaciones Científicas-Universidad Politécnica de Valencia
José Antonio Márquez: European Molecular Biology Laboratory, Grenoble Outstation and Unit of Virus Host-Cell Interactions, UJF-EMBL-CNRS, 6 rue Jules Horowitz, BP181, 38042 Grenoble Cedex 9, France

Nature, 2009, vol. 462, issue 7273, 665-668

Abstract: Abscisic acid: structure of complex with PYR1 The plant hormone abscisic acid (ABA) is an important regulator of plant responses to environmental stresses such as drought and cold. Major players in the ABA signalling pathway include the type 2 phosphatases, ABI1 and ABI2, that negatively regulate ABA responses. Recently a family of proteins known as PYR/PYL/RCAR have been identified, the members of which bind ABA and mediate inactivation of ABI1 and ABI2. Here Márquez and colleagues present the structures of ABA bound to its receptor, PYR1.

Date: 2009
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DOI: 10.1038/nature08591

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