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7cqp
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Complex of TRPC4 and Calmodulin_Nlobe== |
| - | <StructureSection load='7cqp' size='340' side='right'caption='[[7cqp]]' scene=''> | + | <StructureSection load='7cqp' size='340' side='right'caption='[[7cqp]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7cqp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CQP FirstGlance]. <br> |
| - | </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=7cqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cqp OCA], [https://pdbe.org/7cqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cqp RCSB], [https://www.ebi.ac.uk/pdbsum/7cqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cqp ProSAT]</span></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]] 1.9Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7cqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cqp OCA], [https://pdbe.org/7cqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cqp RCSB], [https://www.ebi.ac.uk/pdbsum/7cqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cqp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Drosophila TRP is a calcium-permeable cation channel essential for fly visual signal transduction. During phototransduction, Ca(2+) mediates both positive and negative feedback regulation on TRP channel activity, possibly via binding to calmodulin (CaM). However, the molecular mechanism underlying Ca(2+) modulated CaM/TRP interaction is poorly understood. Here, we discover an unexpected, Ca(2+)-dependent binding mode between CaM and TRP. The TRP tail contains two CaM binding sites (CBS1 and CBS2) separated by an approximately 70-residue linker. CBS1 binds to the CaM N-lobe and CBS2 recognizes the CaM C-lobe. Structural studies reveal the lobe-specific binding of CaM to CBS1&2. Mutations introduced in both CBS1 and CBS2 eliminated CaM binding in full-length TRP, but surprisingly had no effect on the response to light under physiological conditions, suggesting alternative mechanisms governing Ca(2+)-mediated feedback on the channel activity. Finally, we discover that TRPC4, the closest mammalian paralog of Drosophila TRP, adopts a similar CaM binding mode. | ||
| + | |||
| + | Calmodulin binds to Drosophila TRP with an unexpected mode.,Chen W, Shen Z, Asteriti S, Chen Z, Ye F, Sun Z, Wan J, Montell C, Hardie RC, Liu W, Zhang M Structure. 2021 Apr 1;29(4):330-344.e4. doi: 10.1016/j.str.2020.11.016. Epub 2020 , Dec 15. PMID:33326749<ref>PMID:33326749</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7cqp" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| + | [[Category: Shen ZS]] | ||
Current revision
Complex of TRPC4 and Calmodulin_Nlobe
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