2LOV

AR55 solubilised in LPPG micelles

2LOV の概要

• エントリーDOI: 10.2210/pdb2lov/pdb
• 関連するPDBエントリー: 2LOT 2LOU 2LOW
• NMR情報: BMRB: 18226
• 分子名称: Apelin receptor (1 entity in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P35414
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7306.11

構造登録者

Langelaan, D.N.,Rainey, J.K. (登録日: 2012-01-27, 公開日: 2013-01-16, 最終更新日: 2024-05-15)

主引用文献

Langelaan, D.N.,Pandey, A.,Sarker, M.,Rainey, J.K.
Preserved Transmembrane Segment Topology, Structure, and Dynamics in Disparate Micellar Environments.
J Phys Chem Lett, 8:2381-2386, 2017

PubMed Abstract: Detergent micelles are frequently employed as membrane mimetics for solution-state membrane protein nuclear magnetic resonance spectroscopy. Here we compare topology, structure, ps-ns time-scale dynamics, and hydrodynamics of a model protein with one transmembrane (TM) segment (residues 1-55 of the apelin receptor, APJ, a G-protein-coupled receptor) in three distinct, commonly used micellar environments. In each environment, two solvent-protected helical segments connected by a solvent-exposed kink were observed. The break in helical character at the kink was maintained in a helix-stabilizing fluorinated alcohol environment, implying that this structural feature is inherent. Molecular dynamics simulations also substantiate favorable self-assembly of compact protein-micelle complexes with a more dynamic, solvent-exposed kink. Despite the observed similarity in TM segment behavior, micelle-dependent differences were clear in the structure, dynamics, and compactness of the 30-residue, extramembrane N-terminal tail of the protein. This would affect intermolecular interactions and, correspondingly, the functional state of the membrane protein.

PubMed: 28492329
DOI: 10.1021/acs.jpclett.7b00867

実験手法

SOLUTION NMR