3p1p
From Proteopedia
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==Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 peptide== | ==Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 peptide== | ||
| - | <StructureSection load='3p1p' size='340' side='right' caption='[[3p1p]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='3p1p' size='340' side='right'caption='[[3p1p]], [[Resolution|resolution]] 1.95Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3p1p]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3p1p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P1P FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=3p1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1p OCA], [https://pdbe.org/3p1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p1p RCSB], [https://www.ebi.ac.uk/pdbsum/3p1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1p ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | == Disease == |
| - | <table> | + | [https://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN] Intellectual deficit, Birk-Barel type. Birk-Barel mental retardation dysmorphism syndrome (BIBAS) [MIM:[https://omim.org/entry/612292 612292]: A syndrome characterized by mental retardation, hypotonia, hyperactivity, and facial dysmorphism. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:18678320</ref> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/KCNK9_HUMAN KCNK9_HUMAN] pH-dependent, voltage-insensitive, background potassium channel protein.<ref>PMID:11042359</ref> <ref>PMID:11431495</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Small-molecule stabilization of protein-protein interactions is an emerging field in chemical biology. We show how fusicoccanes, originally identified as fungal toxins acting on plants, promote the interaction of 14-3-3 proteins with the human potassium channel TASK-3 and present a semisynthetic fusicoccane derivative (FC-THF) that targets the 14-3-3 recognition motif (mode 3) in TASK-3. In the presence of FC-THF, the binding of 14-3-3 proteins to TASK-3 was increased 19-fold and protein crystallography provided the atomic details of the effects of FC-THF on this interaction. We also tested the functional effects of FC-THF on TASK channels heterologously expressed in Xenopus oocytes. Incubation with 10 muM FC-THF was found to promote the transport of TASK channels to the cell membrane, leading to a significantly higher density of channels at the surface membrane and increased potassium current. | ||
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| + | A semisynthetic fusicoccane stabilizes a protein-protein interaction and enhances the expression of k(+) channels at the cell surface.,Anders C, Higuchi Y, Koschinsky K, Bartel M, Schumacher B, Thiel P, Nitta H, Preisig-Muller R, Schlichthorl G, Renigunta V, Ohkanda J, Daut J, Kato N, Ottmann C Chem Biol. 2013 Apr 18;20(4):583-93. doi: 10.1016/j.chembiol.2013.03.015. PMID:23601647<ref>PMID:23601647</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3p1p" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Anders | + | [[Category: Large Structures]] |
| - | [[Category: Higuchi | + | [[Category: Anders C]] |
| - | [[Category: Kato | + | [[Category: Higuchi Y]] |
| - | [[Category: Ottmann | + | [[Category: Kato N]] |
| - | [[Category: Schumacher | + | [[Category: Ottmann C]] |
| - | [[Category: Thiel | + | [[Category: Schumacher B]] |
| - | + | [[Category: Thiel P]] | |
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Current revision
Crystal structure of human 14-3-3 sigma C38N/N166H in complex with TASK-3 peptide
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Categories: Homo sapiens | Large Structures | Anders C | Higuchi Y | Kato N | Ottmann C | Schumacher B | Thiel P
