2MFR
Solution structure of the transmembrane domain of the insulin receptor in micelles
2MFR の概要
| エントリーDOI | 10.2210/pdb2mfr/pdb |
| NMR情報 | BMRB: 19568 |
| 分子名称 | Insulin receptor (1 entity in total) |
| 機能のキーワード | insulin recepotr, membrane protein, detergent micelles, transferase |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cell membrane; Single-pass type I membrane protein: P06213 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 6716.85 |
| 構造登録者 | |
| 主引用文献 | Li, Q.,Wong, Y.L.,Kang, C. Solution structure of the transmembrane domain of the insulin receptor in detergent micelles Biochim.Biophys.Acta, 1838:1313-1321, 2014 Cited by PubMed Abstract: The insulin receptor (IR) binds insulin and plays important roles in glucose homeostasis by regulating the tyrosine kinase activity at its C-terminus. Its transmembrane domain (TMD) is shown to be important for transferring conformational changes induced by insulin across the cell membrane to regulate kinase activity. In this study, a construct IR(940-988) containing the TMD was expressed and purified for structural studies. Its solution structure in dodecylphosphocholine (DPC) micelles was determined. The sequence containing residues L962 to Y976 of the TMD of the IR in micelles adopts a well-defined helical structure with a kink formed by glycine and proline residues present at its N-terminus, which might be important for its function. Paramagnetic relaxation enhancement (PRE) and relaxation experimental results suggest that residues following the TMD are flexible and expose to aqueous solution. Although purified IR(940-988) in micelles existed mainly as a monomeric form verified by gel filtration and relaxation analysis, cross-linking study suggests that it may form a dimer or oligomers under micelle conditions. PubMed: 24440425DOI: 10.1016/j.bbamem.2014.01.005 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






