3p1o

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilisator Fusicoccin A

Structural highlights

3p1o is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KCNK9_HUMAN Intellectual deficit, Birk-Barel type. Birk-Barel mental retardation dysmorphism syndrome (BIBAS) [MIM: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.^[1]

Function

KCNK9_HUMAN pH-dependent, voltage-insensitive, background potassium channel protein.^[2] ^[3]

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Barel O, Shalev SA, Ofir R, Cohen A, Zlotogora J, Shorer Z, Mazor G, Finer G, Khateeb S, Zilberberg N, Birk OS. Maternally inherited Birk Barel mental retardation dysmorphism syndrome caused by a mutation in the genomically imprinted potassium channel KCNK9. Am J Hum Genet. 2008 Aug;83(2):193-9. PMID:18678320 doi:S0002-9297(08)00410-2
↑ Chapman CG, Meadows HJ, Godden RJ, Campbell DA, Duckworth M, Kelsell RE, Murdock PR, Randall AD, Rennie GI, Gloger IS. Cloning, localisation and functional expression of a novel human, cerebellum specific, two pore domain potassium channel. Brain Res Mol Brain Res. 2000 Oct 20;82(1-2):74-83. PMID:11042359
↑ Vega-Saenz de Miera E, Lau DH, Zhadina M, Pountney D, Coetzee WA, Rudy B. KT3.2 and KT3.3, two novel human two-pore K(+) channels closely related to TASK-1. J Neurophysiol. 2001 Jul;86(1):130-42. PMID:11431495
↑ 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. A semisynthetic fusicoccane stabilizes a protein-protein interaction and enhances the expression of k(+) channels at the cell surface. Chem Biol. 2013 Apr 18;20(4):583-93. doi: 10.1016/j.chembiol.2013.03.015. PMID:23601647 doi:http://dx.doi.org/10.1016/j.chembiol.2013.03.015

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3p1o"

@@ Line 8: / Line 8: @@
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3p1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1o OCA], [https://pdbe.org/3p1o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p1o RCSB], [https://www.ebi.ac.uk/pdbsum/3p1o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1o ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[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/1433S_HUMAN 1433S_HUMAN] Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. When bound to KRT17, regulates protein synthesis and epithelial cell growth by stimulating Akt/mTOR pathway (By similarity).  p53-regulated inhibitor of G2/M progression.
+[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 ==

3p1o

From Proteopedia

Current revision

Crystal structure of human 14-3-3 sigma in complex with TASK-3 peptide and stabilisator Fusicoccin A

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

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