1A4O
14-3-3 PROTEIN ZETA ISOFORM
1A4O の概要
| エントリーDOI | 10.2210/pdb1a4o/pdb |
| 分子名称 | 14-3-3 PROTEIN ZETA (1 entity in total) |
| 機能のキーワード | signal transduction |
| 由来する生物種 | Bos taurus (cattle) |
| 細胞内の位置 | Cytoplasm: P63103 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 111108.37 |
| 構造登録者 | Liu, D.,Bienkowska, J.,Petosa, C.,Collier, R.J.,Fu, H.,Liddington, R.C. (登録日: 1998-02-01, 公開日: 1999-03-02, 最終更新日: 2024-02-07) |
| 主引用文献 | 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 Cited by 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: 7603574DOI: 10.1038/376191a0 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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