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Structure and gating mechanism of the acetylcholine receptor pore
TLDR
An atomic model of the closed pore of the nicotinic acetylcholine receptor, obtained by electron microscopy of crystalline postsynaptic membranes, is presented.
Structural determinants of water permeation through aquaporin-1
TLDR
An atomic model of human red cell AQP1 is described, providing a possible molecular explanation to a longstanding puzzle in physiology—how membranes can be freely permeable to water but impermeable to protons.
Structure of the connexin 26 gap junction channel at 3.5 Å resolution
TLDR
The crystal structure of the gap junction channel formed by human connexin 26 (Cx26), also known as GJB2, is reported at 3.5 Å resolution, and structural determinants of solute transport through the channel are discussed.
Atomic model of plant light-harvesting complex by electron crystallography
The structure of the light-harvesting chlorophyll a/b–protein complex, an integral membrane protein, has been determined at 3.4 Å resolution by electron crystallography of two-dimensional crystals.
Functional role of internal water molecules in rhodopsin revealed by x-ray crystallography
TLDR
The structural model suggests that water molecules, which were observed in the vicinity of highly conserved residues and in the retinal pocket, regulate the activity of rhodopsin-like GPCRs and spectral tuning in visual pigments, respectively.
Nicotinic acetylcholine receptor at 4.6 A resolution: transverse tunnels in the channel wall.
TLDR
It is suggested that the extracellular tunnels are access routes to the binding pockets for ACh, and that the cytoplasmic openings serve as filters to exclude anions and other impermeant species from the vicinity of the pore.
Aquaporin water channels – from atomic structure to clinical medicine
The water permeability of biological membranes has been a longstanding problem in physiology, but the proteins responsible for this remained unknown until discovery of the aquaporin 1 (AQP1) water
Lipid–protein interactions in double-layered two-dimensional AQP0 crystals
TLDR
A 1.9 Å resolution structure of junctional AQP0 is described, determined by electron crystallography of double-layered two-dimensional crystals, which shows that junction formation depends on a conformational switch in an extracellular loop.
Lipid–protein interactions in double-layered two-dimensional AQP0 crystals
Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 Å resolution structure of junctional AQP0, determined by
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