8of8: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)== | |||
<StructureSection load='8of8' size='340' side='right'caption='[[8of8]], [[Resolution|resolution]] 7.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8of8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OF8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=8of8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8of8 OCA], [https://pdbe.org/8of8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8of8 RCSB], [https://www.ebi.ac.uk/pdbsum/8of8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8of8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE] Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), 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.[UniProtKB:P0DP23] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mus musculus]] | |||
[[Category: Oryctolagus cuniculus]] | |||
[[Category: Gravett MSC]] | |||
[[Category: Harlen OG]] | |||
[[Category: Harris SA]] | |||
[[Category: Klebl DP]] | |||
[[Category: Muench SP]] | |||
[[Category: Peckham M]] | |||
[[Category: Read DJ]] | |||
Latest revision as of 08:06, 25 September 2024
Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)Cryo-EM structure of actomyosin-5a-S1 with the full-length lever (nucleotide free)
Structural highlights
FunctionCALM1_MOUSE Calmodulin acts as part of a calcium signal transduction pathway by mediating the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Calcium-binding is required for the activation of calmodulin. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases, such as myosin light-chain kinases and calmodulin-dependent protein kinase type II (CaMK2), 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.[UniProtKB:P0DP23] |
| ||||||||||||||||||