1a4o
From Proteopedia
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'''14-3-3 PROTEIN ZETA ISOFORM''' | '''14-3-3 PROTEIN ZETA ISOFORM''' | ||
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[[Category: Liu, D.]] | [[Category: Liu, D.]] | ||
[[Category: Petosa, C.]] | [[Category: Petosa, C.]] | ||
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Revision as of 06:48, 2 May 2008
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 Page seeded by OCA on Fri May 2 09:48:23 2008
