4GBR
N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor
4GBR の概要
| エントリーDOI | 10.2210/pdb4gbr/pdb |
| 分子名称 | Beta-2 adrenergic receptor, Lysozyme, (2S)-1-(9H-Carbazol-4-yloxy)-3-(isopropylamino)propan-2-ol (3 entities in total) |
| 機能のキーワード | 7 transmembrane helices, g-protein coupled receptor, signal transduction, carazolol, alkylation, membrane, membrane protein-hydrolase complex, membrane protein/hydrolase |
| 由来する生物種 | Homo sapiens (human) 詳細 |
| 細胞内の位置 | Cell membrane; Multi-pass membrane protein: P07550 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 53730.47 |
| 構造登録者 | |
| 主引用文献 | Zou, Y.,Weis, W.I.,Kobilka, B.K. N-terminal t4 lysozyme fusion facilitates crystallization of a g protein coupled receptor. Plos One, 7:e46039-e46039, 2012 Cited by PubMed Abstract: A highly crystallizable T4 lysozyme (T4L) was fused to the N-terminus of the β(2) adrenergic receptor (β(2)AR), a G-protein coupled receptor (GPCR) for catecholamines. We demonstrate that the N-terminal fused T4L is sufficiently rigid relative to the receptor to facilitate crystallogenesis without thermostabilizing mutations or the use of a stabilizing antibody, G protein, or protein fused to the 3rd intracellular loop. This approach adds to the protein engineering strategies that enable crystallographic studies of GPCRs alone or in complex with a signaling partner. PubMed: 23056231DOI: 10.1371/journal.pone.0046039 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.993 Å) |
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