Show simple item record

dc.contributor.authorZeidel, Mark L.
dc.contributor.authorWalz, Thomas
dc.contributor.authorSmith, Barbara L.
dc.contributor.authorAgre, Peter
dc.contributor.authorEngel, Andreas
dc.date.accessioned2010-03-04T20:34:02Z
dc.date.available2010-03-04T20:34:02Z
dc.date.issued1994-01-21
dc.identifier.citationJ Biol Chem. 1994 Jan 21;269(3):1583-6. http://www.jbc.org/content/269/3/1583.longen_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/33899
dc.description.abstractPlasma membranes of several mammalian tissues are highly permeable to water due to the presence of CHIP, the 28-kDa channel-forming integral protein which is the archetypal member of the aquaporin family of water channel proteins. To define its native structure, purified red cell CHIP protein was reconstituted into lipid bilayers at a high protein-to-lipid ratio, and the resulting 3-microns diameter membrane vesicles were examined by high resolution electron microscopy. The reconstituted membranes contained highly ordered two-dimensional crystalline lattices of p422(1) symmetry in which each CHIP tetramer contained a central depression extending from the outer and inner surfaces of the membrane into the transbilayer domain of the molecule. The reconstituted membranes also exhibited extremely high osmotic water permeability, Pf = 0.472 cm/s, corresponding to the sum of activities of all incorporated CHIP molecules. These studies report the first two-dimensional crystallization of a biologically active water channel and provide direct evidence of the structure responsible for its pore-like behavior.en_US
dc.language.isoen_USen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen_US
dc.subjectAquaporinsen_US
dc.subjectErythrocyte Membrane/metabolismen_US
dc.subjectMembrane Proteins/chemistryen_US
dc.titleBiologically active two-dimensional crystals of aquaporin CHIPen_US
dc.typeArticleen_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record