1ih5
From Proteopedia
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| - | [[Image:1ih5.gif|left|200px]] | + | [[Image:1ih5.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF AQUAPORIN-1''' | + | {{Structure |
| + | |PDB= 1ih5 |SIZE=350|CAPTION= <scene name='initialview01'>1ih5</scene>, resolution 3.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF AQUAPORIN-1''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IH5 is a [ | + | 1IH5 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11171962 11171962] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: water channel]] | [[Category: water channel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:17 2008'' |
Revision as of 09:50, 20 March 2008
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| , resolution 3.70Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 11:50:17 2008
