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  • Perspective
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NMR as a tool to investigate the structure, dynamics and function of membrane proteins

Nature Structural & Molecular Biology volume 23, pages 468–474 (2016)Cite this article

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This Perspective provides an overview of recent progress, successes, challenges and future opportunities in the application of solution NMR and solid-state NMR methods to study the structure, dynamics and function of membrane proteins.

Abstract

Membrane-protein NMR occupies a unique niche for determining structures, assessing dynamics, examining folding, and studying the binding of lipids, ligands and drugs to membrane proteins. However, NMR analyses of membrane proteins also face special challenges that are not encountered with soluble proteins, including sample preparation, size limitation, spectral crowding and sparse data accumulation. This Perspective provides a snapshot of current achievements, future opportunities and possible limitations in this rapidly developing field.

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Figure 1: A selection of recent de novo membrane-protein structures determined by solution NMR or ssNMR: OprG (PDB 2N6L), Pseudomonas aeruginosa outer-membrane protein G, a transporter for small amino acids29; YadA (PDB 2LME), Yersinia enterocolitica transmembrane domain of adhesin A, an outer-membrane autotransporter5; pSRII (PDB 2KSY), Natronomonas pharaonis phototaxis receptor sensory rhodopsin II20; TSPO (PDB 2MGY), Mus musculus mitochondrial translocator protein, a cholesterol and porphyrin importer into mitochondria21; and ASR (PDB 2M3G), Anabaena cyanobacterium sensory rhodopsin7.
Figure 2: Membrane-protein function and dynamics, elucidated by NMR.

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Acknowledgements

This work was supported by NIH grants P01 GM72694, R01 GM51329 and R01 AI30557. We thank members of the Tamm laboratory, past and present, for their valuable contributions and R. Nakamoto for helpful discussions.

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  1. Center for Membrane and Cell Physiology, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    Binyong Liang & Lukas K Tamm

  2. Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia, USA

    Binyong Liang & Lukas K Tamm

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Liang, B., Tamm, L. NMR as a tool to investigate the structure, dynamics and function of membrane proteins. Nat Struct Mol Biol 23, 468–474 (2016). https://doi.org/10.1038/nsmb.3226

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