Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR

FEBS Letters

Tamm, Lukas K³  Abildgaard, Frits¹  Bushweller, John H³  Blad, Heike¹  Arora, Ashish² 

[1] NMRFAM, University of Wisconsin, Madison, WI 53706, USA;Molecular and Structural Biology, Central Drug Research Institute, Lucknow 226 001, UP, India;Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22908-0736, USA

关键词: Nuclear magnetic resonance;    Membrane protein;    OmpA;    Influenza hemagglutinin;    Structure–function relation;    Dynamics;   

DOI  :  10.1016/S0014-5793(03)01127-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Recent progress from our laboratories to determine structures of small membrane proteins (up to 20 kDa) in detergent micelles by solution nuclear magnetic resonance (NMR) is reviewed. NMR opens a new window to also study, for the first time, the dynamics of membrane proteins. We report on recent attempts to correlate dynamic measurements on OmpA with the ion channel function of this protein. We also summarize how NMR and spin-label electron paramagnetic resonance spectroscopy and selective mutagenesis can be combined to provide a structural basis towards understanding the mechanism of influenza hemagglutinin-mediated membrane fusion.

【 授权许可】

Unknown