3wg8

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the abscisic acid receptor PYR1 in complex with an antagonist AS6

Structural highlights

3wg8 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PYR1_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.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The plant stress hormone abscisic acid (ABA) is critical for several abiotic stress responses. ABA signaling is normally repressed by group-A protein phosphatases 2C (PP2Cs), but stress-induced ABA binds Arabidopsis PYR/PYL/RCAR (PYL) receptors, which then bind and inhibit PP2Cs. X-ray structures of several receptor-ABA complexes revealed a tunnel above ABA's 3' ring CH that opens at the PP2C binding interface. Here, ABA analogs with sufficiently long 3' alkyl chains were predicted to traverse this tunnel and block PYL-PP2C interactions. To test this, a series of 3'-alkylsulfanyl ABAs were synthesized with different alkyl chain lengths. Physiological, biochemical and structural analyses revealed that a six-carbon alkyl substitution produced a potent ABA antagonist that was sufficiently active to block multiple stress-induced ABA responses in vivo. This study provides a new approach for the design of ABA analogs, and the results validated structure-based design for this target class.

Designed abscisic acid analogs as antagonists of PYL-PP2C receptor interactions.,Takeuchi J, Okamoto M, Akiyama T, Muto T, Yajima S, Sue M, Seo M, Kanno Y, Kamo T, Endo A, Nambara E, Hirai N, Ohnishi T, Cutler SR, Todoroki Y Nat Chem Biol. 2014 Jun;10(6):477-82. doi: 10.1038/nchembio.1524. Epub 2014 May, 4. PMID:24792952^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Santiago J, Rodrigues A, Saez A, Rubio S, Antoni R, Dupeux F, Park SY, Marquez JA, Cutler SR, Rodriguez PL. Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs. Plant J. 2009 Nov;60(4):575-88. doi: 10.1111/j.1365-313X.2009.03981.x. Epub 2009 , Jul 16. PMID:19624469 doi:10.1111/j.1365-313X.2009.03981.x
↑ Park SY, Fung P, Nishimura N, Jensen DR, Fujii H, Zhao Y, Lumba S, Santiago J, Rodrigues A, Chow TF, Alfred SE, Bonetta D, Finkelstein R, Provart NJ, Desveaux D, Rodriguez PL, McCourt P, Zhu JK, Schroeder JI, Volkman BF, Cutler SR. Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteins. Science. 2009 May 22;324(5930):1068-71. doi: 10.1126/science.1173041. Epub 2009, Apr 30. PMID:19407142 doi:10.1126/science.1173041
↑ Szostkiewicz I, Richter K, Kepka M, Demmel S, Ma Y, Korte A, Assaad FF, Christmann A, Grill E. Closely related receptor complexes differ in their ABA selectivity and sensitivity. Plant J. 2010 Jan;61(1):25-35. doi: 10.1111/j.1365-313X.2009.04025.x. Epub 2009, Sep 21. PMID:19769575 doi:10.1111/j.1365-313X.2009.04025.x
↑ Takeuchi J, Okamoto M, Akiyama T, Muto T, Yajima S, Sue M, Seo M, Kanno Y, Kamo T, Endo A, Nambara E, Hirai N, Ohnishi T, Cutler SR, Todoroki Y. Designed abscisic acid analogs as antagonists of PYL-PP2C receptor interactions. Nat Chem Biol. 2014 Jun;10(6):477-82. doi: 10.1038/nchembio.1524. Epub 2014 May, 4. PMID:24792952 doi:http://dx.doi.org/10.1038/nchembio.1524

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3wg8"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the abscisic acid receptor PYR1 in complex with an antagonist AS6==
-<StructureSection load='3wg8' size='340' side='right' caption='[[3wg8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='3wg8' size='340' side='right'caption='[[3wg8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3wg8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WG8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WG8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3wg8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WG8 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6AS:(2Z,4E)-5-[(1S)-3-(HEXYLSULFANYL)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>6AS</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wg8 RCSB], [http://www.ebi.ac.uk/pdbsum/3wg8 PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6AS:(2Z,4E)-5-[(1S)-3-(HEXYLSULFANYL)-1-HYDROXY-2,6,6-TRIMETHYL-4-OXOCYCLOHEX-2-EN-1-YL]-3-METHYLPENTA-2,4-DIENOIC+ACID'>6AS</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg8 OCA], [https://pdbe.org/3wg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wg8 RCSB], [https://www.ebi.ac.uk/pdbsum/3wg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wg8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PYR1_ARATH PYR1_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.<ref>PMID:19624469</ref> <ref>PMID:19407142</ref> <ref>PMID:19769575</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3wg8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Abscisic acid receptor 3D structures|Abscisic acid receptor 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Akiyama, T.]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Cutler, S R.]]
+[[Category: Large Structures]]
-[[Category: Endo, A.]]
+[[Category: Akiyama T]]
-[[Category: Hirai, N.]]
+[[Category: Cutler SR]]
-[[Category: Muto, T.]]
+[[Category: Endo A]]
-[[Category: Nambara, E.]]
+[[Category: Hirai N]]
-[[Category: Ohnishi, T.]]
+[[Category: Muto T]]
-[[Category: Okamoto, M.]]
+[[Category: Nambara E]]
-[[Category: Sue, M.]]
+[[Category: Ohnishi T]]
-[[Category: Takeuchi, J.]]
+[[Category: Okamoto M]]
-[[Category: Todoroki, Y.]]
+[[Category: Sue M]]
-[[Category: Yajima, S.]]
+[[Category: Takeuchi J]]
-[[Category: Abscisic acid]]
+[[Category: Todoroki Y]]
-[[Category: Hormone receptor]]
+[[Category: Yajima S]]

3wg8

From Proteopedia

Current revision

Crystal structure of the abscisic acid receptor PYR1 in complex with an antagonist AS6

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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