6F46

Structure of the transmembrane helix of BclxL in phospholipid nanodiscs

6F46 の概要

• エントリーDOI: 10.2210/pdb6f46/pdb
• NMR情報: BMRB: 27316
• 分子名称: Bcl-2-like protein 1 (1 entity in total)
• 機能のキーワード: nanodiscs, helix, apoptosis
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3878.47

構造登録者

Hagn, F.,Raltchev, K. (登録日: 2017-11-29, 公開日: 2018-07-18, 最終更新日: 2024-06-19)

主引用文献

Raltchev, K.,Pipercevic, J.,Hagn, F.
Production and Structural Analysis of Membrane-Anchored Proteins in Phospholipid Nanodiscs.
Chemistry, 24:5493-5499, 2018

PubMed Abstract: Structural studies on membrane-anchored proteins containing a transmembrane (TM) helix have been hampered by difficulties in producing these proteins in a natively folded form. Detergents that are required to solubilize the hydrophobic TM helix usually destabilize the soluble domain. Thus, TM helices are removed for structural studies, which neglects the pivotal role of a membrane on protein function. This work presents a versatile strategy for the production of this protein class attached to phospholipid nanodiscs. By inserting the TM-helix into nanodiscs and a subsequent SortaseA-mediated ligation of the soluble domain, membrane-anchored BclxL could be obtained in a folded conformation. This strategy is suitable for high-resolution structure determination as well as for probing membrane location by NMR. This method will be applicable to a wide range of membrane-anchored proteins and will be useful to decipher their functional role in a native membrane environment.

PubMed: 29457664
DOI: 10.1002/chem.201800812

実験手法

SOLUTION NMR