Abstract
RELATIVELY LITTLE IS KNOWN about how membrane proteins interact with the lipids that surround them because structural studies typically fail to capture these proteins' lipid environment. Now, a high-resolution structure of a membrane-embedded water channel protein has opened a window to how lipids pack around membrane proteins ( Nature 2005, 438 ,633). key to an effective membrane is to get the packing of the lipids and proteins right, explains Anthony G. Lee of the University of Southampton, England, in an accompanying Nature commentary. The new structural data clearly illustrate how this packing is achieved. Thomas Walz of Harvard Medical School and coworkers captured the 1.9-A structure of aquaporin-0 (AQP0) immersed in an artificial lipid bilayer. AQP0 is a water channel that is the most abundant membrane protein in the lens of the eye. They used electron crystallography, a well-established technique that employs the beam of an electron microscope to produce diffraction patterns from ...
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