4z62: Difference between revisions

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-'''Unreleased structure'''
-The entry 4z62 is ON HOLD
+==The plant peptide hormone free receptor==
+<StructureSection load='4z62' size='340' side='right'caption='[[4z62]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4z62]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Daucus_carota Daucus carota]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z62 FirstGlance]. <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]] 2.9&#8491;</td></tr>
+<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></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4z62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z62 OCA], [https://pdbe.org/4z62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z62 RCSB], [https://www.ebi.ac.uk/pdbsum/4z62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z62 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://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>
+<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.
-Authors: Chai, J.J., Wang, J.Z., Han, Z.F.
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wang, J.Z]]
+<div class="pdbe-citations 4z62" style="background-color:#fffaf0;"></div>
-[[Category: Han, Z.F]]
+== References ==
-[[Category: Chai, J.J]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Daucus carota]]
+[[Category: Large Structures]]
+[[Category: Chai J]]
+[[Category: Han Z]]
+[[Category: Wang J]]