The structural basis for 14-3-3:phosphopeptide binding specificity.
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Summary
It is shown that the 14-3-3 dimer binds tightly to single molecules containing tandem repeats of phosphoserine motifs, implicating bidentate association as a signaling mechanism with molecules such as Raf, BAD, and Cbl.
- Type
- article
- Published
- 1997-12-26
- Cited by
- 1,634
- References
- 48
- Access
- Open access
- OpenAlex
- https://openalex.org/W2071075259
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:14107687
Keywords
Phosphoserine, Phosphopeptide, Biology, Peptide, Dimer
References
- Interaction of the protein kinase Raf-1 with 14-3-3 proteins.
- Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery.
- 14-3-3 alpha and delta are the phosphorylated forms of raf-activating 14-3-3 beta and zeta. In vivo stoichiometric phosphorylation in brain at a Ser-Pro-Glu-Lys MOTIF.
- Protein kinase C inhibitor proteins. Purification from sheep brain and sequence similarity to lipocortins and 14-3-3 protein.
- Principles of Protein Structure
- Molecular cloning and expression of the transformation sensitive epithelial marker stratifin. A member of a protein family that has been involved in the protein kinase C signalling pathway.
- Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations.
- Identification of 14-3-3 proteins in human platelets: effects of synthetic peptides on protein kinase C activation.
- Expression and structural analysis of 14-3-3 proteins.
- Occurrence and role of cis peptide bonds in protein structures.
- Activation-modulated Association of 14–3–3 Proteins with Cbl in T Cells*
- An extensively modified version of MolScript that includes greatly enhanced coloring capabilities.
- Raf-1 Kinase and Exoenzyme S Interact with 14-3-3ζ through a Common Site Involving Lysine 49*
- 14-3-3 Is Phosphorylated by Casein Kinase I on Residue 233
- Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions.
- The CCP4 suite: programs for protein crystallography.
- 14-3-3 and its possible role in co-ordinating multiple signalling pathways.
- RIBBONS 2.0
- Improved methods for building protein models in electron density maps and the location of errors in these models.
- Crystal structure of the zeta isoform of the 14-3-3 protein
Cited by
- Dynamic Regulation at the Neuronal Plasma Membrane: Novel Endocytic Mechanisms Control Anesthetic-Activated Potassium Channels and Amphetamine-Sensitive Dopamine Transporters: A Dissertation
- 14-3-3 proteins and growth control.
- P53-responsive genes and the potential for cancer diagnostics and therapeutics development.
- Functional conservation of 14-3-3 isoforms in inhibiting bad-induced apoptosis.
- Regulation of Raf‐1 activation and signalling by dephosphorylation
- How do 14‐3‐3 proteins work? – Gatekeeper phosphorylation and the molecular anvil hypothesis
- Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase.
- Expression of death‐associated protein kinase and recruitment to the tumor necrosis factor signaling pathway following brief seizures
- 14-3-3-affinity purification of over 200 human phosphoproteins reveals new links to regulation of cellular metabolism, proliferation and trafficking.
- Unlocking the code of 14-3-3
- Phosphoproteomic Analysis of the Developing Mouse Brain*S
- A Role for 14-3-3τ in E2F1 Stabilization and DNA Damage-induced Apoptosis*
- Modulation of subfamily B/R4 RGS protein function by 14-3-3 proteins.
- Scavenging of 14-3-3 proteins reveals their involvement in the cell-surface transport of ATP-sensitive K+ channels
- Structural basis for protein–protein interactions in the 14-3-3 protein family
- The 14-3-3 Proteins: Gene, Gene Expression, and Function
- The regulated assembly of a PKCɛ complex controls the completion of cytokinesis
- Cytosolic RNA recognition pathway activates 14-3-3 protein mediated signaling and caspase-dependent disruption of cytokeratin network in human keratinocytes.
- Structural basis for DNA recognition by FOXO proteins.
- Contribution of PKB/AKT signaling to thyroid cancer.
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