4ehq: Difference between revisions
New page: '''Unreleased structure''' The entry 4ehq is ON HOLD Authors: Liu, Y., Zheng, X., Mueller, G.A., Sobhany, H, DeRose, E.F., Zhang, Y., London, R.E., Birnbaumer, L. Description: Crystal ... |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal Structure of Calmodulin Binding Domain of Orai1 in Complex with Ca2+/Calmodulin Displays a Unique Binding Mode== | |||
<StructureSection load='4ehq' size='340' side='right'caption='[[4ehq]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ehq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EHQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EHQ 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]] 1.9005Å</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>, <scene name='pdbligand=GBL:GAMMA-BUTYROLACTONE'>GBL</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=4ehq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ehq OCA], [https://pdbe.org/4ehq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ehq RCSB], [https://www.ebi.ac.uk/pdbsum/4ehq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ehq ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] 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. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158] | |||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Rattus norvegicus]] | |||
[[Category: Birnbaumer L]] | |||
[[Category: DeRose EF]] | |||
[[Category: Liu Y]] | |||
[[Category: London RE]] | |||
[[Category: Mueller GA]] | |||
[[Category: Sobhany M]] | |||
[[Category: Zhang Y]] | |||
[[Category: Zheng X]] | |||