Journal
NATURE
Volume 462, Issue 7273, Pages 665-U143Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature08591
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Funding
- Ministerio de Educacion y Ciencia [BIO2008-00221]
- Fondo Europeo de Desarrollo Regional
- Consejo Superior de Investigaciones Cientificas
- European Community-Research Infrastructure Action PCUBE
- Division Of Integrative Organismal Systems
- Direct For Biological Sciences [0820508] Funding Source: National Science Foundation
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The plant hormone abscisic acid (ABA) has a central role in coordinating the adaptive response in situations of decreased water availability as well as the regulation of plant growth and development. Recently, a 14-member family of intracellular ABA receptors, named PYR/PYL/RCAR(1-3), has been identified. These proteins inhibit in an ABA-dependent manner the activity of a family of key negative regulators of the ABA signalling pathway: the group-A protein phosphatases type 2C (PP2Cs)(4-6). Here we present the crystal structure of Arabidopsis thaliana PYR1, which consists of a dimer in which one of the subunits is bound to ABA. In the ligand-bound subunit, the loops surrounding the entry to the binding cavity fold over the ABA molecule, enclosing it inside, whereas in the empty subunit they form a channel leaving an open access to the cavity, indicating that conformational changes in these loops have a critical role in the stabilization of the hormone-receptor complex. By providing structural details on the ABA-binding pocket, this work paves the way for the development of new small molecules able to activate the plant stress response.
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