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Cells direct membrane traffic by channel width

were from the same bug, E-coli. One was a pure water channel. The other is a glycerol channel," Tajkhorshid said. "Structurally they are similar. Researchers have tried to convert a water channel to a glycerol channel, or the other way around, by mutating amino acids that line the pore of the channel, but they have failed."

The E-coli proteins studied were AqpZ, a water channel, and GlpF, a glycerol channel. Side-by-side in computer-generated images the channels appear virtually identical. The Beckman teamed pushed glycerol through the channels, calculated the energetics and looked for barriers.

"Nature is using a very, very simple idea here," Tajkhorshid said. "Just by making a channel narrower, only water is allowed to pass through the pure water channel; by making it a little bit bigger in the other channel both glycerol, as well as longer, linear sugar molecules, and water can permeate the channel."

While channel sizes had appeared slightly different after crystallizing the proteins in the past, researchers believed the channels could be manipulated by inducing the surrounding amino acids to create a hydrophobic or semi-hydrophobic lining required for glycerol passage. Success in doing so could have created new targets for drug therapies.

However, it turns out, the amino acids are the same around both channels, Tajkhorshid said. So his team now is looking beyond the amino acids directly lining the channel to find what it is that forces changes in size.

The same principles, he added, likely apply to all selective protein channels. Understanding the principles could provide new, effective pharmaceutical targets to control the channels to help treat disease.

Study co-authors were group director Klaus Schulten and Yi Wang, a doctoral student in molecular and cell biology.


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Source:University of Illinois at Urbana-Champaign


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