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| - | [[Image:1j4n.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1j4n| PDB=1j4n | SCENE= }} | | {{STRUCTURE_1j4n| PDB=1j4n | SCENE= }} |
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| - | '''Crystal Structure of the AQP1 water channel'''
| + | ===Crystal Structure of the AQP1 water channel=== |
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| - | ==Overview==
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| - | Water channels facilitate the rapid transport of water across cell membranes in response to osmotic gradients. These channels are believed to be involved in many physiological processes that include renal water conservation, neuro-homeostasis, digestion, regulation of body temperature and reproduction. Members of the water channel superfamily have been found in a range of cell types from bacteria to human. In mammals, there are currently 10 families of water channels, referred to as aquaporins (AQP): AQP0-AQP9. Here we report the structure of the aquaporin 1 (AQP1) water channel to 2.2 A resolution. The channel consists of three topological elements, an extracellular and a cytoplasmic vestibule connected by an extended narrow pore or selectivity filter. Within the selectivity filter, four bound waters are localized along three hydrophilic nodes, which punctuate an otherwise extremely hydrophobic pore segment. This unusual combination of a long hydrophobic pore and a minimal number of solute binding sites facilitates rapid water transport. Residues of the constriction region, in particular histidine 182, which is conserved among all known water-specific channels, are critical in establishing water specificity. Our analysis of the AQP1 pore also indicates that the transport of protons through this channel is highly energetically unfavourable.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11780053}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11780053 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11780053}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Membrane protein]] | | [[Category: Membrane protein]] |
| | [[Category: Transmembrane helice]] | | [[Category: Transmembrane helice]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:47:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:29:41 2008'' |
Revision as of 11:29, 1 July 2008
Template:STRUCTURE 1j4n
Crystal Structure of the AQP1 water channel
Template:ABSTRACT PUBMED 11780053
About this Structure
1J4N is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Structural basis of water-specific transport through the AQP1 water channel., Sui H, Han BG, Lee JK, Walian P, Jap BK, Nature. 2001 Dec 20-27;414(6866):872-8. PMID:11780053
Page seeded by OCA on Tue Jul 1 14:29:41 2008
