4z61
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The | + | ==The plant peptide hormone receptor complex== |
| + | <StructureSection load='4z61' size='340' side='right' caption='[[4z61]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4z61]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z61 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z61 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TYS:O-SULFO-L-TYROSINE'>TYS</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4z5w|4z5w]], [[4z62|4z62]], [[4z63|4z63]], [[4z64|4z64]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=4z61 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z61 OCA], [http://pdbe.org/4z61 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z61 RCSB], [http://www.ebi.ac.uk/pdbsum/4z61 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PSKR1_DAUCA PSKR1_DAUCA]] Phytosulfokine receptor with a serine/threonine-protein kinase activity. Regulates, in response to phytosulfokine binding, a signaling cascade involved in plant cell differentiation, organogenesis and somatic embryogenesis.<ref>PMID:12029134</ref> [[http://www.uniprot.org/uniprot/SERK2_ARATH SERK2_ARATH]] Serine/threonine-kinase involved in brassinosteroid-dependent and -independent signaling pathways. Acts redundantly with SERK1 as a control point for sporophytic development controlling male gametophyte production.<ref>PMID:18667726</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phytosulfokine (PSK) is a disulfated pentapeptide that has a ubiquitous role in plant growth and development. PSK is perceived by its receptor PSKR, a leucine-rich repeat receptor kinase (LRR-RK). The mechanisms underlying the recognition of PSK, the activation of PSKR and the identity of the components downstream of the initial binding remain elusive. Here we report the crystal structures of the extracellular LRR domain of PSKR in free, PSK- and co-receptor-bound forms. The structures reveal that PSK interacts mainly with a beta-strand from the island domain of PSKR, forming an anti-beta-sheet. The two sulfate moieties of PSK interact directly with PSKR, sensitizing PSKR recognition of PSK. Supported by biochemical, structural and genetic evidence, PSK binding enhances PSKR heterodimerization with the somatic embryogenesis receptor-like kinases (SERKs). However, PSK is not directly involved in PSKR-SERK interaction but stabilizes PSKR island domain for recruitment of a SERK. Our data reveal the structural basis for PSKR recognition of PSK and allosteric activation of PSKR by PSK, opening up new avenues for the design of PSKR-specific small molecules. | ||
| - | + | Allosteric receptor activation by the plant peptide hormone phytosulfokine.,Wang J, Li H, Han Z, Zhang H, Wang T, Lin G, Chang J, Yang W, Chai J Nature. 2015 Sep 10;525(7568):265-8. doi: 10.1038/nature14858. Epub 2015 Aug 26. PMID:26308901<ref>PMID:26308901</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4z61" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Non-specific serine/threonine protein kinase]] | ||
| + | [[Category: Chai, J]] | ||
| + | [[Category: Wang, J]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Hormone receptor]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:04, 2 March 2016
The plant peptide hormone receptor complex
| |||||||||||
