3rgx

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{{STRUCTURE_3rgx| PDB=3rgx | SCENE= }}
 
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===Structural insight into brassinosteroid perception by BRI1===
 
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{{ABSTRACT_PUBMED_21666666}}
 
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==About this Structure==
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==Structural insight into brassinosteroid perception by BRI1==
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[[3rgx]] is a 1 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=3RGX OCA].
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<StructureSection load='3rgx' size='340' side='right'caption='[[3rgx]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3rgx]] 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=3RGX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RGX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.47&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rgx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rgx OCA], [https://pdbe.org/3rgx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rgx RCSB], [https://www.ebi.ac.uk/pdbsum/3rgx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rgx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BRI1_ARATH BRI1_ARATH] Receptor with a dual specificity kinase activity acting on both serine/threonine- and tyrosine-containing substrates. Regulates, in response to brassinosteroid binding, a signaling cascade involved in plant development, including expression of light- and stress-regulated genes, promotion of cell elongation, normal leaf and chloroplast senescence, and flowering. Binds brassinolide, and less effectively castasterone, but not 2,3,22,23-O-tetramethylbrassinolide or ecdysone. May be involved in a feedback regulation of brassinosteroid biosynthesis. Phosphorylates BRI1-associated receptor kinase 1 (BAK1), Transthyretin-Like protein (TTL) and SERK1 on 'Ser-299' and 'Thr-462' in vitro. May have a guanylyl cyclase activity.<ref>PMID:10557222</ref> <ref>PMID:10938344</ref> <ref>PMID:17138891</ref> <ref>PMID:17520012</ref> <ref>PMID:18694562</ref> <ref>PMID:19124768</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Brassinosteroids are essential phytohormones that have crucial roles in plant growth and development. Perception of brassinosteroids requires an active complex of BRASSINOSTEROID-INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE 1 (BAK1). Recognized by the extracellular leucine-rich repeat (LRR) domain of BRI1, brassinosteroids induce a phosphorylation-mediated cascade to regulate gene expression. Here we present the crystal structures of BRI1(LRR) in free and brassinolide-bound forms. BRI1(LRR) exists as a monomer in crystals and solution independent of brassinolide. It comprises a helical solenoid structure that accommodates a separate insertion domain at its concave surface. Sandwiched between them, brassinolide binds to a hydrophobicity-dominating surface groove on BRI1(LRR). Brassinolide recognition by BRI1(LRR) is through an induced-fit mechanism involving stabilization of two interdomain loops that creates a pronounced non-polar surface groove for the hormone binding. Together, our results define the molecular mechanisms by which BRI1 recognizes brassinosteroids and provide insight into brassinosteroid-induced BRI1 activation.
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==Reference==
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Structural insight into brassinosteroid perception by BRI1.,She J, Han Z, Kim TW, Wang J, Cheng W, Chang J, Shi S, Wang J, Yang M, Wang ZY, Chai J Nature. 2011 Jun 12;474(7352):472-6. doi: 10.1038/nature10178. PMID:21666666<ref>PMID:21666666</ref>
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<ref group="xtra">PMID:021666666</ref><references group="xtra"/><references/>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rgx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
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[[Category: Chai, J.]]
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[[Category: Large Structures]]
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[[Category: Cheng, W.]]
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[[Category: Chai J]]
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[[Category: Han, Z.]]
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[[Category: Cheng W]]
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[[Category: She, J.]]
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[[Category: Han Z]]
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[[Category: Wang, J.]]
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[[Category: She J]]
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[[Category: Brassinosteroid]]
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[[Category: Wang J]]
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[[Category: Leucine-rich repeat]]
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[[Category: Leucine-rich repeat receptor-like kinase]]
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[[Category: Phytohormone]]
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[[Category: Transferase]]
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Current revision

Structural insight into brassinosteroid perception by BRI1

PDB ID 3rgx

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