2002 Global Researcher Conference Proceeding
April 26 - 28, 2002
| Conference: | 2002 Global Researcher Conference |
|---|---|
| Title: | Progress in the function and structure of aquaporin-1 and aquaporin-2 |
| Authors: | Fotiadis, PhD, Dimitrios; Werten, Paul J.L.; Suda, Kitaru; Schenk, Andreas; Frederix, Patrick; Scheuring, Simon; Stahlberg, Henning; Engel, Andreas |
| Institutions: | Maurice E. Mueller Institute Biozentrum der Universitat Basel, Maurice E. Mueller Institute for Microscopy, Biozentrum of the University of Basel, Maurice E. Mueller Institute at the Biozentrum |
Aquaporins are membrane channels involved in osmoregulation in bacteria, plants and animals. In the latter, aquaporin-2 (AQP2) is found in the collecting duct cells of the kidney and is regulated by the antidiuretic hormone vasopressin. We have grown highly ordered, biologically active two-dimensional (2D) crystals of recombinant human AQP21 and determined its structure by cryo-electron microscopy and atomic force microscopy (AFM). Compared to AQP2, the tissue distribution of aquaporin-1 (AQP1) in animals is much broader. By AFM we have mapped the location of the C-terminus of AQP1 using 2D crystals of native bovine and human AQP1 and have found a Ca2+ binding site at its C-terminus2 in contrast to the putative cyclic guanosine monophosphate binding site previously reported3.
- Werten, P. J., Hasler, L., Koenderink, J. B., Klaassen, C. H., de Grip, W. J., Engel, A. & Deen, P. M. (2001). Large-scale purification of functional recombinant human aquaporin-2. FEBS Letters 504, 200-205.
- Fotiadis, D., Suda, K., Tittmann, P., Jenö, P., Philippsen, A., Müller, D. J., Gross, H. & Engel, A. (2002). Identification and structure of a putative Ca2+ binding domain at the C-terminus of AQP1. J. Mol. Biol. in press.
- Anthony, T. L., Brooks, H. L., Boassa, D., Leonov, S., Yanochko, G. M., Regan, J. W. & Yool, A. J. (2000). Cloned human aquaporin-1 is a cyclic GMP-gated ion channel. Mol. Pharmacol. 57, 576-588.



