1ih5

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Current revision (07:35, 7 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ih5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hw0 1hw0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IH5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ih5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1hw0 1hw0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IH5 FirstGlance]. <br>
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</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=1ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ih5 OCA], [https://pdbe.org/1ih5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ih5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ih5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ih5 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ih5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ih5 OCA], [https://pdbe.org/1ih5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ih5 RCSB], [https://www.ebi.ac.uk/pdbsum/1ih5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ih5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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>
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[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=1ih5 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=1ih5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:11171962</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1ih5" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cheng, A]]
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[[Category: Cheng A]]
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[[Category: Melnyk, P]]
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[[Category: Melnyk P]]
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[[Category: Mitra, A K]]
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[[Category: Mitra AK]]
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[[Category: Reddy, V S]]
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[[Category: Reddy VS]]
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[[Category: Ren, G]]
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[[Category: Ren G]]
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[[Category: Membrane protein]]
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[[Category: Two-dimensional crystal]]
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[[Category: Water channel]]
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Current revision

CRYSTAL STRUCTURE OF AQUAPORIN-1

PDB ID 1ih5

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