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3j41

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Pseudo-atomic model of the Aquaporin-0/Calmodulin complex derived from electron microscopy

3j41, resolution 25.00Å

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@@ Line 3: / Line 3: @@
 <SX load='3j41' size='340' side='right' viewer='molstar' caption='[[3j41]], [[Resolution|resolution]] 25.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3j41]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J41 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3j41]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J41 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 25&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b6p|2b6p]], [[1nwd|1nwd]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2, CAM3, CAMC, CAMIII ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3j41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j41 OCA], [https://pdbe.org/3j41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j41 RCSB], [https://www.ebi.ac.uk/pdbsum/3j41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j41 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/MIP_SHEEP MIP_SHEEP] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.<ref>PMID:15141214</ref> <ref>PMID:15351655</ref> <ref>PMID:20389283</ref>
-Calmodulin (CaM) is a universal regulatory protein that communicates the presence of calcium to its molecular targets and correspondingly modulates their function. This key signaling protein is important for controlling the activity of hundreds of membrane channels and transporters. However, understanding of the structural mechanisms driving CaM regulation of full-length membrane proteins has remained elusive. In this study, we determined the pseudoatomic structure of full-length mammalian aquaporin-0 (AQP0, Bos taurus) in complex with CaM, using EM to elucidate how this signaling protein modulates water-channel function. Molecular dynamics and functional mutation studies reveal how CaM binding inhibits AQP0 water permeability by allosterically closing the cytoplasmic gate of AQP0. Our mechanistic model provides new insight, only possible in the context of the fully assembled channel, into how CaM regulates multimeric channels by facilitating cooperativity between adjacent subunits.
-Allosteric mechanism of water-channel gating by Ca-calmodulin.,Reichow SL, Clemens DM, Freites JA, Nemeth-Cahalan KL, Heyden M, Tobias DJ, Hall JE, Gonen T Nat Struct Mol Biol. 2013 Jul 28. doi: 10.1038/nsmb.2630. PMID:23893133<ref>PMID:23893133</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3j41" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 17: @@
 __TOC__
 </SX>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
 [[Category: Ovis aries]]
-[[Category: Clemens, D M]]
+[[Category: Clemens DM]]
-[[Category: Freites, J A]]
+[[Category: Freites JA]]
-[[Category: Gonen, T]]
+[[Category: Gonen T]]
-[[Category: Hall, J E]]
+[[Category: Hall JE]]
-[[Category: Heyden, M]]
+[[Category: Heyden M]]
-[[Category: Nemeth-Cahalan, K L]]
+[[Category: Nemeth-Cahalan KL]]
-[[Category: Reichow, S L]]
+[[Category: Reichow SL]]
-[[Category: Tobias, D J]]
+[[Category: Tobias DJ]]
-[[Category: Calcium regulation]]
-[[Category: Membrane protein complex]]
-[[Category: Transport protein-calcium binding complex]]
-[[Category: Water channel]]

3j41

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Current revision

Pseudo-atomic model of the Aquaporin-0/Calmodulin complex derived from electron microscopy

Structural highlights

Function

See Also

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