1ih5
From Proteopedia
(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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| - | [[Image:1ih5.gif|left|200px]]<br /> | + | [[Image:1ih5.gif|left|200px]]<br /><applet load="1ih5" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ih5" size=" | + | |
caption="1ih5, resolution 3.70Å" /> | caption="1ih5, resolution 3.70Å" /> | ||
'''CRYSTAL STRUCTURE OF AQUAPORIN-1'''<br /> | '''CRYSTAL STRUCTURE OF AQUAPORIN-1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The water-selective pathway through the aquaporin-1 membrane channel has | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IH5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure | + | 1IH5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1HW0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IH5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cheng, A.]] | [[Category: Cheng, A.]] | ||
[[Category: Melnyk, P.]] | [[Category: Melnyk, P.]] | ||
| - | [[Category: Mitra, A | + | [[Category: Mitra, A K.]] |
| - | [[Category: Reddy, V | + | [[Category: Reddy, V S.]] |
[[Category: Ren, G.]] | [[Category: Ren, G.]] | ||
[[Category: electron microscopy]] | [[Category: electron microscopy]] | ||
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[[Category: water channel]] | [[Category: water channel]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:49 2008'' |
Revision as of 11:11, 21 February 2008
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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 supersedes 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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