1fqy
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The May 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Aquaporin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_5 10.2210/rcsb_pdb/mom_2014_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQY FirstGlance]. <br> | <table><tr><td colspan='2'>[[1fqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The May 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Aquaporin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_5 10.2210/rcsb_pdb/mom_2014_5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQY FirstGlance]. <br> | ||
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqy OCA], [https://pdbe.org/1fqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqy RCSB], [https://www.ebi.ac.uk/pdbsum/1fqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqy ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 3.8Å</td></tr> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqy OCA], [https://pdbe.org/1fqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqy RCSB], [https://www.ebi.ac.uk/pdbsum/1fqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/AQP1_HUMAN AQP1_HUMAN] Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.<ref>PMID:1373524</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqy ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqy ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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<ref>PMID:11034202</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1fqy" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
| - | [[Category: Agre | + | [[Category: Agre P]] |
| - | [[Category: Engel | + | [[Category: Engel A]] |
| - | [[Category: Fujiyoshi | + | [[Category: Fujiyoshi Y]] |
| - | [[Category: Heymann | + | [[Category: Heymann JB]] |
| - | [[Category: Hirai | + | [[Category: Hirai T]] |
| - | [[Category: Mitsuoka | + | [[Category: Mitsuoka K]] |
| - | [[Category: Murata | + | [[Category: Murata K]] |
| - | [[Category: Walz | + | [[Category: Walz T]] |
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Current revision
STRUCTURE OF AQUAPORIN-1 AT 3.8 A RESOLUTION BY ELECTRON CRYSTALLOGRAPHY
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