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| Figure 5: Mercury inhibition of the aquaporin-Z monomer in stereo. The surface of the protein and its aqueous pathway can clearly be seen in conjunction with the location of Hg1 and Hg2 as well as pertinent residues contributing to their stability. Hg1 can clearly be seen (in red) sitting in the aqueous pathway, sterically blocking the movement of water. His-174 (orange) and Ser-184 (yellow), which electrostaticly bond with Hg1 are also present. Hg2 (also in red) can be seen on the interior of the protein bonded to the T183C mutant (Accession code 209E). |