3SP5
Crystal structure of human 14-3-3 sigma C38V/N166H in complex with TASK-3 peptide and stabilizer Cotylenol
Summary for 3SP5
| Entry DOI | 10.2210/pdb3sp5/pdb |
| Related | 2O98 3IQU 3LW1 |
| Descriptor | 14-3-3 protein sigma, TASK-3 peptide, Cotylenol, ... (5 entities in total) |
| Functional Keywords | helical protein, phosphoprotein, adapter protein, peptide binding protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cytoplasm: P31947 |
| Total number of polymer chains | 2 |
| Total formula weight | 27761.95 |
| Authors | Anders, C.,Schumacher, B.,Ottmann, C. (deposition date: 2011-07-01, release date: 2016-05-04, Last modification date: 2024-10-09) |
| Primary citation | 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., 20:583-593, 2013 Cited by PubMed Abstract: 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 μM 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. PubMed: 23601647DOI: 10.1016/j.chembiol.2013.03.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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