Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
Membrane proteins are central to many physiological processes and are targeted by ~50% of marketed pharmaceutical drugs. Determining the structures of membrane proteins is essential for understanding their function and for drug design. This Focus highlights the latest breakthroughs in elucidating the structure and mechanisms of ABC transporters and neurotransmitter-gated ion channels; it also explores recent technical and methodological advances in X-ray crystallography, cryo-EM, NMR and computational approaches to investigate membrane proteins.
In a common yet effective analogy, a cell can be compared to a fortified city, in which lipid membranes form the defensive walls, and membrane proteins function as gates and checkpoints that control the transit of molecules and information across these walls. We evoke this concept on the cover of this special Focus on Membrane Proteins.
Wayne Hendrickson discusses the consortium efforts and developments in methodology that in recent years have allowed unprecedented advances in atomic-structure determination of membrane proteins.
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.
This Perspective provides an overview of the major advances in recent years in the computational design and structure prediction of α-helical membrane proteins.
The use of nanodiscs is substantially fostering structural and functional studies of membrane protein. This Perspective summarizes the recent use of nanodiscs as an invaluable tool for the characterization of membrane proteins.
ABC transporters use ATP hydrolysis to translocate substrates across cell membranes. Kaspar Locher reviews the mechanistic diversity of ABC transporters, as has emerged from recent structural studies, and discusses future directions for investigation of ABC-transporter-catalyzed reactions.
Numerous recent crystal and cryo-EM structures have greatly advanced understanding of the functional mechanisms of neurotransmitter-gated ion channels. This Review discusses the structural basis of activation and desensitization mechanisms in glutamate and cysteine-loop receptors.