1h6i

<StructureSection load='1h6i' size='340' side='right' caption='[[1h6i]], [[Resolution|resolution]] 3.54&Aring;' scene=''>

<table><tr><td colspan='2'>[[1h6i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H6I FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fqy|1fqy]], [[1hw0|1hw0]], [[1ih5|1ih5]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6i OCA], [http://pdbe.org/1h6i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h6i RCSB], [http://www.ebi.ac.uk/pdbsum/1h6i PDBsum]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h6/1h6i_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

A refined structure of the human water channel aquaporin-1 is presented. The model rests on the high resolution X-ray structure of the homologous bacterial glycerol transporter GlpF, electron crystallographic data at 3.8 A resolution and a multiple sequence alignment of the aquaporin superfamily. The crystallographic R and free R values (36.7% and 37.8%) for the refined structure are significantly lower than for previous models. Improved geometry and enhanced stability in molecular dynamics simulations demonstrate a significant improvement of the aquaporin-1 structure. Comparison with previous aquaporin-1 models shows significant differences, not only in the loop regions, but also in the core of the water channel.

A refined structure of human aquaporin-1.,de Groot BL, Engel A, Grubmuller H FEBS Lett. 2001 Aug 31;504(3):206-11. PMID:11532455<ref>PMID:11532455</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1h6i" style="background-color:#fffaf0;"></div>

[[Category: Engel, A]]

[[Category: Groot, B L.De]]

[[Category: Grubmuller, H]]

[[Category: Membrane protein]]

[[Category: Water channel]]