Structural highlights
4dhu is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
|
| Ligands: | , , , |
| NonStd Res: | |
| Related: | 3t0l, 3t0m, 3u9x, 4dhm, 4dhn, 4dho, 4dhp, 4dhq, 4dhr, 4dhs, 4dht |
| Gene: | HME1, SFN (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[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.
Publication Abstract from PubMed
We report first non-covalent and exclusively extracellular inhibitors of 14-3-3 protein-protein interactions identified by virtual screening. Optimization by crystal structure analysis and in vitro binding assays yielded compounds capable of disrupting the interaction of 14-3-3sigma with aminopeptidase N in a cellular assay.
Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 protein-protein interactions.,Thiel P, Roglin L, Meissner N, Hennig S, Kohlbacher O, Ottmann C Chem Commun (Camb). 2013 Aug 27;49(76):8468-70. doi: 10.1039/c3cc44612c. PMID:23939230[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Thiel P, Roglin L, Meissner N, Hennig S, Kohlbacher O, Ottmann C. Virtual screening and experimental validation reveal novel small-molecule inhibitors of 14-3-3 protein-protein interactions. Chem Commun (Camb). 2013 Aug 27;49(76):8468-70. doi: 10.1039/c3cc44612c. PMID:23939230 doi:10.1039/c3cc44612c
