3gd8: Difference between revisions

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<StructureSection load='3gd8' size='340' side='right'caption='[[3gd8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3gd8' size='340' side='right'caption='[[3gd8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3gd8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3GD8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3gd8]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3GD8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AQP4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3gd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gd8 OCA], [https://pdbe.org/3gd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gd8 RCSB], [https://www.ebi.ac.uk/pdbsum/3gd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gd8 ProSAT]</span></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=3gd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gd8 OCA], [https://pdbe.org/3gd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gd8 RCSB], [https://www.ebi.ac.uk/pdbsum/3gd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gd8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/AQP4_HUMAN AQP4_HUMAN]] Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system.  
[https://www.uniprot.org/uniprot/AQP4_HUMAN AQP4_HUMAN] Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system.
== 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=3gd8 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=3gd8 ConSurf].
<div style="clear:both"></div>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3gd8" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Aquaporin 3D structures|Aquaporin 3D structures]]
*[[Aquaporin 3D structures|Aquaporin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: CSMP, Center for Structures of Membrane Proteins]]
[[Category: Chorny I]]
[[Category: Chorny, I]]
[[Category: Harries WEC]]
[[Category: Harries, W E.C]]
[[Category: Ho JD]]
[[Category: Ho, J D]]
[[Category: Miercke LJW]]
[[Category: Miercke, L J.W]]
[[Category: Robbins RA]]
[[Category: Robbins, R A]]
[[Category: Sandstrom A]]
[[Category: Sandstrom, A]]
[[Category: Stroud RM]]
[[Category: Stroud, R M]]
[[Category: Yeh R]]
[[Category: Yeh, R]]
[[Category: Aquaporin]]
[[Category: Brain edema]]
[[Category: Center for structures of membrane protein]]
[[Category: Csmp]]
[[Category: Glycoprotein]]
[[Category: Membrane]]
[[Category: Membrane protein]]
[[Category: Phosphoprotein]]
[[Category: PSI, Protein structure initiative]]
[[Category: Proton exclusion]]
[[Category: Structural genomic]]
[[Category: Transmembrane]]
[[Category: Transport]]

Latest revision as of 12:53, 21 February 2024

Crystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of ConductanceCrystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of Conductance

Structural highlights

3gd8 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AQP4_HUMAN Forms a water-specific channel. Osmoreceptor which regulates body water balance and mediates water flow within the central nervous system.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3gd8, resolution 1.80Å

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