3gd8
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of Conductance== | |
- | + | <StructureSection load='3gd8' size='340' side='right' caption='[[3gd8]], [[Resolution|resolution]] 1.80Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3gd8]] 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=3GD8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GD8 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AQP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3gd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gd8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gd8 RCSB], [http://www.ebi.ac.uk/pdbsum/3gd8 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gd/3gd8_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Aquaporin (AQP) 4 is the predominant water channel in the mammalian brain, abundantly expressed in the blood-brain and brain-cerebrospinal fluid interfaces of glial cells. Its function in cerebral water balance has implications in neuropathological disorders, including brain edema, stroke, and head injuries. The 1.8-A crystal structure reveals the molecular basis for the water selectivity of the channel. Unlike the case in the structures of water-selective AQPs AqpZ and AQP1, the asparagines of the 2 Asn-Pro-Ala motifs do not hydrogen bond to the same water molecule; instead, they bond to 2 different water molecules in the center of the channel. Molecular dynamics simulations were performed to ask how this observation bears on the proposed mechanisms for how AQPs remain totally insulating to any proton conductance while maintaining a single file of hydrogen bonded water molecules throughout the channel. | ||
- | + | Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance.,Ho JD, Yeh R, Sandstrom A, Chorny I, Harries WE, Robbins RA, Miercke LJ, Stroud RM Proc Natl Acad Sci U S A. 2009 May 5;106(18):7437-42. Epub 2009 Apr 21. PMID:19383790<ref>PMID:19383790</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
*[[Aquaporin|Aquaporin]] | *[[Aquaporin|Aquaporin]] | ||
*[[Aquaporin 4|Aquaporin 4]] | *[[Aquaporin 4|Aquaporin 4]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: CSMP, Center for Structures of Membrane Proteins | + | [[Category: CSMP, Center for Structures of Membrane Proteins]] |
- | [[Category: Chorny, I | + | [[Category: Chorny, I]] |
- | [[Category: Harries, W E.C | + | [[Category: Harries, W E.C]] |
- | [[Category: Ho, J D | + | [[Category: Ho, J D]] |
- | [[Category: Miercke, L J.W | + | [[Category: Miercke, L J.W]] |
- | [[Category: Robbins, R A | + | [[Category: Robbins, R A]] |
- | [[Category: Sandstrom, A | + | [[Category: Sandstrom, A]] |
- | [[Category: Stroud, R M | + | [[Category: Stroud, R M]] |
- | [[Category: Yeh, R | + | [[Category: Yeh, R]] |
[[Category: Aquaporin]] | [[Category: Aquaporin]] | ||
[[Category: Brain edema]] | [[Category: Brain edema]] | ||
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[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Phosphoprotein]] | [[Category: Phosphoprotein]] | ||
- | [[Category: Protein structure initiative]] | + | [[Category: PSI, Protein structure initiative]] |
[[Category: Proton exclusion]] | [[Category: Proton exclusion]] | ||
- | [[Category: Psi-2]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Transport]] | [[Category: Transport]] |
Revision as of 14:09, 17 December 2014
Crystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of Conductance
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Categories: Homo sapiens | CSMP, Center for Structures of Membrane Proteins | Chorny, I | Harries, W E.C | Ho, J D | Miercke, L J.W | Robbins, R A | Sandstrom, A | Stroud, R M | Yeh, R | Aquaporin | Brain edema | Center for structures of membrane protein | Csmp | Glycoprotein | Membrane | Membrane protein | Phosphoprotein | PSI, Protein structure initiative | Proton exclusion | Structural genomic | Transmembrane | Transport