Article
Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons.
Proceedings of the National Academy of Sciences of the United States of America - 10 Jan 2006
Beitz Eric, Wu Binghua, Holm Lars M, Schultz Joachim E, Zeuthen Thomas
Abstract excerpt
Water-specific aquaporins (AQP), such as the prototypical mammalian AQP1, stringently exclude the passage of solutes, ions, and even protons. Supposedly, this is accomplished by two conserved regions within the pore, a pair of canonical asparagine-proline-alanine (NPA) motifs, the central constriction, and an aromatic/arginine (ar/R) constriction, the outer constriction. Here, we analyzed the function of three...
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