1fqy
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(New page: 200px<br /> <applet load="1fqy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fqy, resolution 3.80Å" /> '''STRUCTURE OF AQUAPO...)
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Revision as of 14:50, 12 November 2007
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STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY
Contents |
Overview
Human red cell AQP1 is the first functionally defined member of the, aquaporin family of membrane water channels. Here we describe an atomic, model of AQP1 at 3.8A resolution from electron crystallographic data., Multiple highly conserved amino-acid residues stabilize the novel fold of, AQP1. The aqueous pathway is lined with conserved hydrophobic residues, that permit rapid water transport, whereas the water selectivity is due to, a constriction of the pore diameter to about 3 A over a span of one, residue. The atomic model provides a possible molecular explanation to a, longstanding puzzle in physiology-how membranes can be freely permeable to, water but impermeable to protons.
Disease
Known diseases associated with this structure: Aquaporin-1 deficiency OMIM:[107776], Blood group, Colton OMIM:[107776]
About this Structure
1FQY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural determinants of water permeation through aquaporin-1., Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y, Nature. 2000 Oct 5;407(6804):599-605. PMID:11034202
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