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Research Digest Synopses of Research Articles Structure of Aquaporin Reveals Mechanism for Transport Selectivity Biochemists aren’t much accustomed to seeing their work in the popular press, save for annual coverage of the Nobel prize in chemistry.This year, Roderick MacKinnon was recognized for working out the atomic structure of an ion channel and Peter Agre for discovering that a major protein found in red blood cells functions primarily as a water channel. Agre went on to establish the family of related channels, which he named“aquaporins.’’ After fabricating and growing a recombinant form of AqpZ in E. coli, David Savage in the Stroud group recovered the proteins from the bacterial colonies, then puri?ed and concentrated them. The proteins were crystallized—capturing ?ve water molecules inside—and then analyzed by state-of-the-art high-resolution X-ray diffraction techniques.The architecture of aquaporin Z, the researchers report, is typical of aquaporins, with a spiral of eight oxygens providing water-binding sites inside the channel and amino acid side chains determining the size and chemistry of the channel.The outer membrane and cytoplasmic Channel proteins have aqueous membrane and regulate the ?ow of molecules in and out of cells.Water passively pours though aquaporins by osmosis, moving from low to high concentrations pores that cross the cell ends of the channel are wider than the interior, which is long and narrow. of solutes. Solving This structure con?rms the structure of these that aquaporin selectivity channels provided a arises in part from erecting platform for exploring a physical barrier: small the underlying molecular mechanisms that allow molecules, like water, can easily pass, but larger ones the proteins to function as ?lters and maintain osmotic equilibrium. Robert Stroud and colleagues recently solved the atomic structure of an aquaporin (GlpF) and have now solved the structure of another water channel from Escherichia coli, called a