C-terminal Binding: an Expanded Repertoire and Function of 14-3-3 Proteins.
From: Department of Neuroscience and High Throughput Biology Center, School of Medicine, Johns Hopkins University, 733 North Broadway, Baltimore, MD 21205, USA.
FEBS letters
- Publish Date: Mar 2006
- ISSN: 0014-5793
- Volume: 580
- Issue: 6
- Pages: 1531-5
- Medium: Print
- Language: English
- Citation (JAMA): Coblitz Brian, Wu Meng, Shikano Sojin, et al. C-terminal Binding: an Expanded Repertoire and Function of 14-3-3 Proteins.. FEBS Lett. Mar 2006;580:1531-5
Abstract
Amino and carboxyl termini are unique positions in a polypeptide. They tend to be exposed in folded three dimensional structures. Diversity and functional significance of C-terminal sequences have been appreciated from studies of PDZ and PEX domains. Signaling 14-3-3 protein signaling by recognizing phosphorylated peptides plays a critical role in a variety of biological processes, including oncogenesis. The preferential binding of 14-3-3 to phosphorylated C-terminal sequences, mode III, provides a means of regulated binding and considerably expands the substrate repertoire of 14-3-3 interaction partners.
Mesh Headings (Keywords): 14-3-3 Proteins, Amino Acid Motifs, Animals, Binding Sites, Consensus Sequence, Humans, Protein Binding, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 16494877
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