Please use this identifier to cite or link to this item: https://doi.org/10.1038/nsmb.1887
Title: Identification and mechanism of ABA receptor antagonism
Authors: Melcher, K.
Xu, Y.
Ng, L.-M.
Zhou, X.E.
Soon, F.-F.
Chinnusamy, V.
Suino-Powell, K.M.
Kovach, A.
Tham, F.S.
Cutler, S.R.
Li, J. 
Yong, E.-L. 
Zhu, J.-K.
Xu, H.E.
Issue Date: Sep-2010
Citation: Melcher, K., Xu, Y., Ng, L.-M., Zhou, X.E., Soon, F.-F., Chinnusamy, V., Suino-Powell, K.M., Kovach, A., Tham, F.S., Cutler, S.R., Li, J., Yong, E.-L., Zhu, J.-K., Xu, H.E. (2010-09). Identification and mechanism of ABA receptor antagonism. Nature Structural and Molecular Biology 17 (9) : 1102-1108. ScholarBank@NUS Repository. https://doi.org/10.1038/nsmb.1887
Abstract: The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands. © 2010 Nature America, Inc. All rights reserved.
Source Title: Nature Structural and Molecular Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/126999
ISSN: 15459993
DOI: 10.1038/nsmb.1887
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

85
checked on Jun 16, 2018

WEB OF SCIENCETM
Citations

75
checked on May 29, 2018

Page view(s)

15
checked on May 17, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.