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First published online January 16, 2009
Journal of Experimental Biology 212, 358-362 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.024794
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The role of aquaporins in excretion in insects

Jeffrey H. Spring1,*, S. Renee Robichaux2 and John A. Hamlin2

1 Department of Biology, University of Louisiana at Lafayette, Lafayette, LA 70504, USA
2 Division of Sciences, Louisiana State University at Eunice, Eunice, LA 70535, USA


Figure 1
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  		Fig. 1. Primary structure of human AQP1. The six transmembrane domains are shown as they are inserted in the membrane with the five connecting loops (A–E) linking them. The NPA (Asn–Pro–Ala) motifs in loops B and E are shown as well as cysteine 189 and alanine 73, which are the primary and secondary sites for mercury inhibition. After Agre et al. (Agre et al., 1993Go). For further details, see text.

 

Figure 2
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  		Fig. 2. The hourglass model for the folding of human AQP1. The six transmembrane domains consist of two tandem repeats and fold to form the central water-transporting pore. The cytoplasmic connecting loop B and the extracellular loop E, which contain the NPA motifs, fold inwards to meet in the center of the pore, forming the primary proton filter. C, Cys189; A, Ala73. After Jung et al. (Jung et al., 1994Go).

 

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© The Company of Biologists Ltd 2009