4lsx

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{{STRUCTURE_4lsx| PDB=4lsx | SCENE= }}
 
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===Plant steroid receptor ectodomain bound to brassinolide and SERK1 co-receptor ectodomain===
 
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{{ABSTRACT_PUBMED_23929946}}
 
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==Function==
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==Plant steroid receptor ectodomain bound to brassinolide and SERK1 co-receptor ectodomain==
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[[http://www.uniprot.org/uniprot/SERK1_ARATH SERK1_ARATH]] Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Phosphorylates BRI1 on 'Ser-887' and CDC48 on at least one threonine residue and on 'Ser-41'. Confers embryogenic competence. Acts redundantly with SERK2 as a control point for sporophytic development controlling male gametophyte production. Involved in the brassinolide signaling pathway.<ref>PMID:11509554</ref> <ref>PMID:17693538</ref>
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<StructureSection load='4lsx' size='340' side='right'caption='[[4lsx]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4lsx]] is a 4 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=4LSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LSX 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]] 3.302&#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=BLD:BRASSINOLIDE'>BLD</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=4lsx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lsx OCA], [https://pdbe.org/4lsx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lsx RCSB], [https://www.ebi.ac.uk/pdbsum/4lsx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lsx 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, which control plant growth and development, are sensed by the leucine-rich repeat (LRR) domain of the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1), but it is unknown how steroid binding at the cell surface activates the cytoplasmic kinase domain of the receptor. A family of somatic embryogenesis receptor kinases (SERKs) has been genetically implicated in mediating early brassinosteroid signaling events. We found a direct and steroid-dependent interaction between the BRI1 and SERK1 LRR domains by analysis of their complex crystal structure at 3.3 angstrom resolution. We show that the SERK1 LRR domain is involved in steroid sensing and, through receptor-co-receptor heteromerization, in the activation of the BRI1 signaling pathway. Our work reveals how known missense mutations in BRI1 and in SERKs modulate brassinosteroid signaling and the targeting mechanism of BRI1 receptor antagonists.
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==About this Structure==
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Molecular mechanism for plant steroid receptor activation by somatic embryogenesis co-receptor kinases.,Santiago J, Henzler C, Hothorn M Science. 2013 Aug 23;341(6148):889-92. doi: 10.1126/science.1242468. Epub 2013, Aug 8. PMID:23929946<ref>PMID:23929946</ref>
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[[4lsx]] is a 4 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=4LSX OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:023929946</ref><references group="xtra"/><references/>
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</div>
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<div class="pdbe-citations 4lsx" 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: Henzler, C.]]
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[[Category: Large Structures]]
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[[Category: Hothorn, M.]]
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[[Category: Henzler C]]
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[[Category: Santiago, J.]]
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[[Category: Hothorn M]]
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[[Category: Brassinosteroid binding]]
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[[Category: Santiago J]]
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[[Category: Lrr-domain]]
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[[Category: Membrane signaling complex receptor co-receptor complex]]
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[[Category: N-glycosylation]]
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[[Category: Steroid binding protein-protein binding complex]]
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Current revision

Plant steroid receptor ectodomain bound to brassinolide and SERK1 co-receptor ectodomain

PDB ID 4lsx

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