4e53: Difference between revisions
New page: '''Unreleased structure''' The entry 4e53 is ON HOLD Authors: Veerendra Kumar , Jayaraman Sivaraman Description: Calmodulin and Nm peptide complex |
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==Calmodulin and Nm peptide complex== | |||
<StructureSection load='4e53' size='340' side='right'caption='[[4e53]], [[Resolution|resolution]] 2.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4e53]] 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=4E53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E53 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69Å</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=4e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e53 OCA], [https://pdbe.org/4e53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [https://www.ebi.ac.uk/pdbsum/4e53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e53 ProSAT]</span></td></tr> | |||
</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/NEUM_MOUSE NEUM_MOUSE] This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.[UniProtKB:P17677] | |||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Kumar V]] | |||
[[Category: Sivaraman J]] | |||
Latest revision as of 11:49, 20 March 2024
Calmodulin and Nm peptide complexCalmodulin and Nm peptide complex
Structural highlights
FunctionCALM1_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]NEUM_MOUSE This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.[UniProtKB:P17677] See Also |
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