4e50: Difference between revisions

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<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4e50]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E50 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E50 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4e50]] is a 1 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=4E50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E50 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e53|4e53]]</td></tr>
</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=4e50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e50 OCA], [https://pdbe.org/4e50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [https://www.ebi.ac.uk/pdbsum/4e50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e50 ProSAT]</span></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=4e50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e50 OCA], [http://pdbe.org/4e50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [http://www.ebi.ac.uk/pdbsum/4e50 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e50 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][[https://www.uniprot.org/uniprot/NEUG_MOUSE NEUG_MOUSE]] Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.<ref>PMID:11016969</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kumar, V]]
[[Category: Mus musculus]]
[[Category: Sivaraman, J]]
[[Category: Kumar V]]
[[Category: Intrinsically unstructured protein]]
[[Category: Sivaraman J]]
[[Category: Iq motif]]
[[Category: Neurogranin]]
[[Category: Protein binding]]
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