3w9r

<StructureSection load='3w9r' size='340' side='right'caption='[[3w9r]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[3w9r]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W9R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W9R FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A8S:(2Z,4E)-5-[(1S)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>A8S</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3w9r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w9r OCA], [https://pdbe.org/3w9r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w9r RCSB], [https://www.ebi.ac.uk/pdbsum/3w9r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w9r ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/PYL9_ARATH PYL9_ARATH]] Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA. Confers enhanced sensitivity to ABA.<ref>PMID:19407143</ref>

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== Publication Abstract from PubMed ==

Arabidopsis receptors of abscisic acid (ABA), the key plant hormone for adaptation to water stress, comprise 14 PYR/PYLs/RCARs proteins classified into three subfamilies I, II, and III, which suggests functional differentiation. Although their monomer-dimer equilibria may be correlated with differences in their ABA-binding affinities, how the dimerization decreases the affinity is unclear. Comparative structural and binding studies between PYL9, which is a representative of high-affinity subfamily I, and low-affinity members of subfamily III reveals that the nonpolar triplet (Ile110, Val162, and Leu165) and Pro64 contribute to enhance ABA-binding affinity by inducing a shift of the ABA carboxyl group to form additional direct hydrogen bonds with conserved Asn169. Our mutation studies of PYL1 successfully produced a monomeric mutant PYL1 exhibiting low ABA affinity and also a dimeric mutant PYL1 exhibiting high ABA-binding affinity, suggesting that dimer formation of ABA receptors is not essential for their low ABA-binding affinity. Our study contributes toward establishing the structural basis for the higher ABA-binding affinity of the subfamily receptors and provides a clue for understanding the broad spectrum of hormone actions in plants manifested by the different hormone-binding affinity of multiple receptors.

Mechanism of high-affinity abscisic acid binding to PYL9/RCAR1.,Nakagawa M, Kagiyama M, Shibata N, Hirano Y, Hakoshima T Genes Cells. 2014 Mar 19. doi: 10.1111/gtc.12140. PMID:24645846<ref>PMID:24645846</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3w9r" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Hakoshima, T]]

[[Category: Hirano, Y]]

[[Category: Kagiyama, M]]

[[Category: Nakagawa, M]]

[[Category: Shibata, N]]

[[Category: Start/bet v1 family]]