3gd8: Difference between revisions
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==Crystal Structure of Human Aquaporin 4 at 1.8 and its Mechanism of Conductance== | ==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=''> | <StructureSection load='3gd8' size='340' side='right'caption='[[3gd8]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3gd8]] is a 1 chain structure with sequence from [ | <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> | ||
</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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AQP4 ([ | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Aquaporin|Aquaporin | *[[Aquaporin 3D structures|Aquaporin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: CSMP, Center for Structures of Membrane Proteins]] | [[Category: CSMP, Center for Structures of Membrane Proteins]] | ||
[[Category: Chorny, I]] | [[Category: Chorny, I]] | ||
Revision as of 11:02, 9 March 2022
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
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. Publication Abstract from PubMedAquaporin (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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Human
- Large Structures
- 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