2LOW

Solution structure of AR55 in 50% HFIP

Summary for 2LOW

• Entry DOI: 10.2210/pdb2low/pdb
• Related: 2LOT 2LOU 2LOW
• NMR Information: BMRB: 18227
• Descriptor: Apelin receptor (1 entity in total)
• Functional Keywords: membrane protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Multi-pass membrane protein: P35414
• Total number of polymer chains: 1
• Total formula weight: 7306.11

Authors

Langelaan, D.N.,Rainey, J.K. (deposition date: 2012-01-27, release date: 2013-01-16, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR