1a4o

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Revision as of 08:29, 20 November 2007

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spinqualitylabelsall models 1a4o, resolution 2.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

14-3-3 PROTEIN ZETA ISOFORM

Overview

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.

About this Structure

1A4O is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the zeta isoform of the 14-3-3 protein., Liu D, Bienkowska J, Petosa C, Collier RJ, Fu H, Liddington R, Nature. 1995 Jul 13;376(6536):191-4. PMID:7603574

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