7odk
From Proteopedia
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==Plant peptide hormone receptor H1== | ==Plant peptide hormone receptor H1== | ||
| - | <StructureSection load='7odk' size='340' side='right'caption='[[7odk]]' scene=''> | + | <StructureSection load='7odk' size='340' side='right'caption='[[7odk]], [[Resolution|resolution]] 1.83Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ODK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ODK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7odk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ODK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ODK FirstGlance]. <br> |
| - | </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=7odk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7odk OCA], [https://pdbe.org/7odk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7odk RCSB], [https://www.ebi.ac.uk/pdbsum/7odk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7odk ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7odk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7odk OCA], [https://pdbe.org/7odk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7odk RCSB], [https://www.ebi.ac.uk/pdbsum/7odk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7odk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The membrane receptor kinases HAESA and HSL2 recognize a family of IDA/IDL signaling peptides to control cell separation processes in different plant organs. The homologous HSL1 has been reported to regulate epidermal cell patterning by interacting with a different class of signaling peptides from the CLE family. Here we demonstrate that HSL1 binds IDA/IDL peptides with high, and CLE peptides with lower affinity, respectively. Ligand sensing capability and receptor activation of HSL1 require a SERK co-receptor kinase. Crystal structures with IDA/IDLs or with CLE9 reveal that HSL1-SERK1 complex recognizes the entire IDA/IDL signaling peptide, while only parts of CLE9 are bound to the receptor. In contrast, the receptor kinase BAM1 interacts with the entire CLE9 peptide with high affinity and specificity. Furthermore, the receptor tandem BAM1/BAM2 regulates epidermal cell division homeostasis. Consequently, HSL1-IDLs and BAM1/BAM2-CLEs independently regulate cell patterning in the leaf epidermal tissue. | ||
| + | |||
| + | HSL1 and BAM1/2 impact epidermal cell development by sensing distinct signaling peptides.,Roman AO, Jimenez-Sandoval P, Augustin S, Broyart C, Hothorn LA, Santiago J Nat Commun. 2022 Feb 15;13(1):876. doi: 10.1038/s41467-022-28558-4. PMID:35169143<ref>PMID:35169143</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7odk" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Jimenez-Sandoval P]] | + | [[Category: Non-specific serine/threonine protein kinase]] |
| - | [[Category: Roman | + | [[Category: Jimenez-Sandoval, P]] |
| - | [[Category: Santiago J]] | + | [[Category: Roman, A O]] |
| + | [[Category: Santiago, J]] | ||
| + | [[Category: Peptide binding protein]] | ||
| + | [[Category: Plant receptor lrr pepide hormone]] | ||
Revision as of 07:29, 2 March 2022
Plant peptide hormone receptor H1
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