Aquaporin 10 paralogs exhibit evolutionarily altered urea and boric acid permeabilities based on the amino acid residues at positions 1 and 3 in the ar/R region
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Abstract
Urea and boric acid permeabilities of aquaporin (Aqp)-10.2 are lower than those of Aqp10.1 and plesiomorphic Aqp10, and the molecular weight sum of the two amino acid residues in the aromatic/arginine (ar/R) selectivity filter plays a filtering role that affects permeability. Therefore, urea and boric acid permeabilities of Aqp10s can be assessed using the sum of the molecular weights of the two amino acids in the ar/R region, which represents a significant advancement in this field.
