Small molecules, peptides and natural products: getting a grip on 14-3-3 protein-protein modulation

One of the proteins that is found in a diverse range of eukaryotic protein-protein interactions is the adaptor protein 14-3-3. As 14-3-3 is a hub protein with very diverse interactions, it is a good model to study various protein-protein interactions. A wide range of classes of molecules, peptides,...

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Bibliographic Details
Published in:Future medicinal chemistry Vol. 6; no. 8; p. 903
Main Authors: Bartel, Maria, Schäfer, Anja, Stevers, Loes M, Ottmann, Christian
Format: Journal Article
Language:English
Published: England 01.05.2014
Subjects:
14-3-3 Proteins - chemistry
14-3-3 Proteins - metabolism
Binding Sites
Biological Products - chemistry
Biological Products - metabolism
Humans
Peptides - chemistry
Peptides - metabolism
Protein Interaction Domains and Motifs
Protein Structure, Tertiary
Small Molecule Libraries - chemistry
Small Molecule Libraries - metabolism
ISSN:1756-8927, 1756-8927
Online Access:Get more information
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Summary:One of the proteins that is found in a diverse range of eukaryotic protein-protein interactions is the adaptor protein 14-3-3. As 14-3-3 is a hub protein with very diverse interactions, it is a good model to study various protein-protein interactions. A wide range of classes of molecules, peptides, small molecules or natural products, has been used to modify the protein interactions, providing both stabilization or inhibition of the interactions of 14-3-3 with its binding partners. The first protein crystal structures were solved in 1995 and gave molecular insights for further research. The plant analog of 14-3-3 binds to a plant plasma membrane H(+)-ATPase and this protein complex is stabilized by the fungal phytotoxin fusicoccin A. The knowledge gained from the process in plants was transferred to and applied in human models to find stabilizers or inhibitors of 14-3-3 interaction in human cellular pathways.
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ISSN:1756-8927
1756-8927
DOI:10.4155/fmc.14.47