Title : Inhibition of aquaporin-1 water permeability by tetraethylammonium: involvement of the loop E pore region.

Pub. Date : 2000 May

PMID : 10779387






3 Functional Relationships(s)
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1 For AQP1, inhibition by mercury has been attributed to the formation of a mercaptide bond with cysteine residue 189 found in the putative pore-forming region loop E. Here we show that the nonmercurial compound, tetraethylammonium (TEA) chloride, reduces the water permeability of human AQP1 channels expressed in Xenopus oocytes. Mercury aquaporin 1 (Colton blood group) Homo sapiens
2 For AQP1, inhibition by mercury has been attributed to the formation of a mercaptide bond with cysteine residue 189 found in the putative pore-forming region loop E. Here we show that the nonmercurial compound, tetraethylammonium (TEA) chloride, reduces the water permeability of human AQP1 channels expressed in Xenopus oocytes. Mercury aquaporin 1 (Colton blood group) Homo sapiens
3 Using polymerase chain reaction, tyrosine 186 in AQP1, selected for its proximity to the mercury-binding site, was mutated to phenylalanine (Y186F), alanine (Y186A), or asparagine (Y186N). Mercury aquaporin 1 (Colton blood group) Homo sapiens