1ih5
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(New page: 200px<br /> <applet load="1ih5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ih5, resolution 3.70Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:23, 12 November 2007
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CRYSTAL STRUCTURE OF AQUAPORIN-1
Contents |
Overview
The water-selective pathway through the aquaporin-1 membrane channel has, been visualized by fitting an atomic model to a 3.7-A resolution, three-dimensional density map. This map was determined by analyzing images, and electron diffraction patterns of lipid-reconstituted two-dimensional, crystals of aquaporin-1 preserved in vitrified buffer in the absence of, any additive. The aqueous pathway is characterized by a size-selective, pore that is approximately 4.0 +/- 0.5A in diameter, spans a length of, approximately 18A, and bends by approximately 25 degrees as it traverses, the bilayer. This narrow pore is connected by wide, funnel-shaped openings, at the extracellular and cytoplasmic faces. The size-selective pore is, outlined mostly by hydrophobic residues, resulting in a relatively inert, pathway conducive to diffusion-limited water flow. The apex of the curved, pore is close to the locations of the in-plane pseudo-2-fold symmetry axis, that relates the N- and C-terminal halves and the conserved, functionally, important N76 and N192 residues.
Disease
Known diseases associated with this structure: Aquaporin-1 deficiency OMIM:[107776], Blood group, Colton OMIM:[107776]
About this Structure
1IH5 is a Single protein structure of sequence from Homo sapiens. This structure superseeds the now removed PDB entry 1HW0. Full crystallographic information is available from OCA.
Reference
Visualization of a water-selective pore by electron crystallography in vitreous ice., Ren G, Reddy VS, Cheng A, Melnyk P, Mitra AK, Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1398-403. Epub 2001 Jan 30. PMID:11171962
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