1A4O

14-3-3 PROTEIN ZETA ISOFORM

Summary for 1A4O

• Entry DOI: 10.2210/pdb1a4o/pdb
• Descriptor: 14-3-3 PROTEIN ZETA (1 entity in total)
• Functional Keywords: signal transduction
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P63103
• Total number of polymer chains: 4
• Total formula weight: 111108.37

Authors

Liu, D.,Bienkowska, J.,Petosa, C.,Collier, R.J.,Fu, H.,Liddington, R.C. (deposition date: 1998-02-01, release date: 1999-03-02, Last modification date: 2024-02-07)

Primary citation

Liu, D.,Bienkowska, J.,Petosa, C.,Collier, R.J.,Fu, H.,Liddington, R.
Crystal structure of the zeta isoform of the 14-3-3 protein.
Nature, 376:191-194, 1995

PubMed Abstract: The 14-3-3 family of proteins have recently been identified as regulatory elements in intracellular signalling pathways: 14-3-3 proteins bind to oncogene and proto-oncogene products, including c-Raf-1 (refs 2-5), c-Bcr (ref. 6) and polyomavirus middle-T antigen; overexpression of 14-3-3 activates Raf kinase in yeast and induces meiotic maturation in Xenopus oocytes. Here we report the crystal structure of the major isoform of mammalian 14-3-3 proteins at 2.9 A resolution. Each subunit of the dimeric protein consists of a bundle of nine antiparallel helices that form a palisade around an amphipathic groove. The groove is large enough to accommodate a tenth helix, and we propose that binding to an amphipathic helix represents a general mechanism for the interaction of 14-3-3 with diverse cellular proteins. The residues in the dimer interface and the putative ligand-binding surface are invariant among vertebrates, yeast and plants, suggesting a conservation of structure and function throughout the 14-3-3 family.

PubMed: 7603574
DOI: 10.1038/376191a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)