3nmh: Difference between revisions
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==Crystal structure of the abscisic receptor PYL2 in complex with pyrabactin== | |||
<StructureSection load='3nmh' size='340' side='right' caption='[[3nmh]], [[Resolution|resolution]] 1.85Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3nmh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NMH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=PYV:4-BROMO-N-(PYRIDIN-2-YLMETHYL)NAPHTHALENE-1-SULFONAMIDE'>PYV</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nmn|3nmn]], [[3nmp|3nmp]], [[3nmt|3nmt]], [[3nmv|3nmv]], [[3kaz|3kaz]], [[3kb0|3kb0]], [[3kb3|3kb3]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PYL2, RCAR14, At2g26040, T19L18.15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nmh RCSB], [http://www.ebi.ac.uk/pdbsum/3nmh PDBsum]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nm/3nmh_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Identification and mechanism of ABA receptor antagonism.,Melcher K, Xu Y, Ng LM, Zhou XE, Soon FF, Chinnusamy V, Suino-Powell KM, Kovach A, Tham FS, Cutler SR, Li J, Yong EL, Zhu JK, Xu HE Nat Struct Mol Biol. 2010 Sep;17(9):1102-8. Epub 2010 Aug 22. PMID:20729862<ref>PMID:20729862</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[PYR/PYL/RCAR family of ABA receptors|PYR/PYL/RCAR family of ABA receptors]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Kovach, A | [[Category: Kovach, A]] | ||
[[Category: Li, J | [[Category: Li, J]] | ||
[[Category: Melcher, K | [[Category: Melcher, K]] | ||
[[Category: Ng, L M | [[Category: Ng, L M]] | ||
[[Category: Soon, F F | [[Category: Soon, F F]] | ||
[[Category: Suino-Powell, K M | [[Category: Suino-Powell, K M]] | ||
[[Category: Xu, H E | [[Category: Xu, H E]] | ||
[[Category: Xu, Y | [[Category: Xu, Y]] | ||
[[Category: Yong, E L | [[Category: Yong, E L]] | ||
[[Category: Zhou, X E | [[Category: Zhou, X E]] | ||
[[Category: Abscisic acid]] | [[Category: Abscisic acid]] | ||
[[Category: Helix-grip fold]] | [[Category: Helix-grip fold]] | ||
Revision as of 10:05, 19 December 2014
Crystal structure of the abscisic receptor PYL2 in complex with pyrabactinCrystal structure of the abscisic receptor PYL2 in complex with pyrabactin
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Identification and mechanism of ABA receptor antagonism.,Melcher K, Xu Y, Ng LM, Zhou XE, Soon FF, Chinnusamy V, Suino-Powell KM, Kovach A, Tham FS, Cutler SR, Li J, Yong EL, Zhu JK, Xu HE Nat Struct Mol Biol. 2010 Sep;17(9):1102-8. Epub 2010 Aug 22. PMID:20729862[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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