Aquaporins Protein Structure

Description

Description of aquaporins secondary, tertiary and quaternary structure. The secondary form is composed of 6 transmembrane alpha helices and 5 loops. These helices fold into a channel with an NPA (amino acids) motif at its center, forming the pore. 4 subunits form the tetrameric quaternary form of the aquaporin.

Acknowledgements

References

Walz, T., T. Hirai, K. Murata, J.B. Heymann, K. Mitsuoka, Y. Fujiyoshi, B.L. Smith, P. Agre, and A. Engel. 1997. The three-dimensional structure of aquaporin-1. Nature. 387:624-627. Murata, K., K. Mitsuoka, T. Hirai, T. Walz, P. Agre, J.B. Heymann, A. Engel, and Y. Fujiyoshi. 2000. Structural determinants of water permeation through aquaporin-1. Nature. 407:599-605. Hofinger, S., E. Yamamoto, Y. Hirano, F. Zerbetto, T. Narumi, K. Yasuoka, and M. Yasui. 2012. Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes. Biochim Biophys Acta. 1818:2234-2243.

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