1PMS
PLECKSTRIN HOMOLOGY DOMAIN OF SON OF SEVENLESS 1 (SOS1) WITH GLYCINE-SERINE ADDED TO THE N-TERMINUS, NMR, 20 STRUCTURES
1PMS の概要
| エントリーDOI | 10.2210/pdb1pms/pdb |
| 分子名称 | SOS 1 (1 entity in total) |
| 機能のキーワード | pleckstrin, son of sevenless, signal transduction, riken structural genomics/proteomics initiative, rsgi, structural genomics |
| 由来する生物種 | Mus musculus (house mouse) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 15571.88 |
| 構造登録者 | Koshiba, S.,Kigawa, T.,Kim, J.,Shirouzu, M.,Bowtell, D.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 1997-02-18, 公開日: 1997-05-15, 最終更新日: 2024-05-22) |
| 主引用文献 | Koshiba, S.,Kigawa, T.,Kim, J.H.,Shirouzu, M.,Bowtell, D.,Yokoyama, S. The solution structure of the pleckstrin homology domain of mouse Son-of-sevenless 1 (mSos1). J.Mol.Biol., 269:579-591, 1997 Cited by PubMed Abstract: The solution structure of the pleckstrin homology (PH) domain of mouse Son-of-sevenless 1 (mSos1), a guanine nucleotide exchange factor for Ras, was determined by multidimensional NMR spectroscopy. The structure of the mSos1 PH domain involves the fundamental PH fold, consisting of seven beta-strands and one alpha-helix at the C terminus, as determined for the PH domains of other proteins. By contrast, the mSos1 PH domain showed two major characteristic features. First, the N-terminal region, whose amino acid sequence is highly conserved among Sos proteins, was found to form an alpha-helix, which interacts with the beta-sheet structure of the fundamental PH fold. Second, there is a long unstructured loop between beta3 and beta4. Furthermore, the mSos1 PH domain was found to bind phosphatidylinositol-4,5-bisphosphate by a centrifugation assay. The addition of inositol-1,4,5-trisphosphate to the mSos1 PH domain induced backbone amide chemical shift changes mainly in the beta1/beta2 loop and the N- and C-terminal parts of the long beta3/beta4 loop. This inositol-1,4,5-trisphosphate-binding mode of the mSos1 PH domain is somewhat similar to those of the PH domains of pleckstrin and phospholipase Cdelta1, and is clearly different from those of other PH domains. PubMed: 9217262DOI: 10.1006/jmbi.1997.1041 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
構造検証レポート
検証レポート(詳細版)
をダウンロード






