The three-dimensional structure of aquaporin-1

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dc.contributor.author Engel, Andreas
dc.contributor.author Agre, Peter
dc.contributor.author Smith, Barbara L.
dc.contributor.author Fujiyoshi, Yoshinori
dc.contributor.author Mitsuoka, Kaoru
dc.contributor.author Heymann, J. Bernard
dc.contributor.author Murata, Kazuyoshi
dc.contributor.author Hirai, Teruhisa
dc.contributor.author Walz, Thomas
dc.date.accessioned 2010-05-13T18:08:52Z
dc.date.available 2010-05-13T18:08:52Z
dc.date.issued 1997-06-05
dc.identifier.citation Nature 387, 624-627 (5 June 1997) | doi:10.1038/42512 en
dc.identifier.uri http://jhir.library.jhu.edu/handle/1774.2/34114
dc.description.abstract The entry and exit of water from cells is a fundamental process of life. Recognition of the high water permeability of red blood cells led to the proposal that specialized water pores exist in the plasma membrane. Expression in Xenopus oocytes and functional studies of an erythrocyte integral membrane protein of relative molecular mass 28,000, identified it as the mercury-sensitive water channel, aquaporin-1 (AQP1). Many related proteins, all belonging to the major intrinsic protein (MIP) family, are found throughout nature. AQP1 is a homotetramer containing four independent aqueous channels. When reconstituted into lipid bilayers, the protein forms two-dimensional lattices with a unit cell containing two tetramers in opposite orientation. Here we present the three-dimensional structure of AQP1 determined at 6A resolution by cryo-electron microscopy. Each AQP1 monomer has six tilted, bilayer-spanning alpha-helices which form a right-handed bundle surrounding a central density. These results, together with functional studies, provide a model that identifies the aqueous pore in the AQP1 molecule and indicates the organization of the tetrameric complex in the membrane. en
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dc.language.iso en_US en
dc.publisher Nature Publishing Group en
dc.subject Protein Conformation en
dc.subject Ion Channels/chemistry en
dc.subject Aquaporins en
dc.title The three-dimensional structure of aquaporin-1 en
dc.type Article en

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