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| | <StructureSection load='5hit' size='340' side='right'caption='[[5hit]], [[Resolution|resolution]] 2.85Å' scene=''> | | <StructureSection load='5hit' size='340' side='right'caption='[[5hit]], [[Resolution|resolution]] 2.85Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5hit]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HIT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HIT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5hit]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HIT FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM, CAM, RCJMB04_24e7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK]), Kcnh1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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'>[http://proteopedia.org/fgij/fg.htm?mol=5hit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hit OCA], [http://pdbe.org/5hit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hit RCSB], [http://www.ebi.ac.uk/pdbsum/5hit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hit ProSAT]</span></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=5hit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hit OCA], [https://pdbe.org/5hit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hit RCSB], [https://www.ebi.ac.uk/pdbsum/5hit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hit ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | + | [https://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Marques-Carvalho, M J]] | + | [[Category: Marques-Carvalho MJ]] |
| - | [[Category: Morais-Cabral, J H]] | + | [[Category: Morais-Cabral JH]] |
| - | [[Category: Calmodulin]]
| + | |
| - | [[Category: Potassium channel]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
CALM_CHICK Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Publication Abstract from PubMed
The human EAG1 potassium channel belongs to the superfamily of KCNH voltage-gated potassium channels that have roles in cardiac repolarization and neuronal excitability. EAG1 is strongly inhibited by Ca2+/calmodulin (CaM) through a mechanism that is not understood. We determined the binding properties of CaM with each one of three previously identified binding sites (BDN, BDC1, and BDC2), analyzed binding to protein stretches that include more than one site, and determined the effect of neighboring globular domains on the binding properties. The determination of the crystal structure of CaM bound to BDC2 shows the channel fragment interacting with only the C lobe of calmodulin and adopting an unusual bent conformation. Based on this structure and on a functional and biochemical analysis of mutants, we propose a model for the mechanism of inhibition whereby the local conformational change induced by CaM binding at BDC2 lies at the basis of channel modulation.
Molecular Insights into the Mechanism of Calmodulin Inhibition of the EAG1 Potassium Channel.,Marques-Carvalho MJ, Oppermann J, Munoz E, Fernandes AS, Gabant G, Cadene M, Heinemann SH, Schonherr R, Morais-Cabral JH Structure. 2016 Sep 7. pii: S0969-2126(16)30234-9. doi:, 10.1016/j.str.2016.07.020. PMID:27618660[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Marques-Carvalho MJ, Oppermann J, Munoz E, Fernandes AS, Gabant G, Cadene M, Heinemann SH, Schonherr R, Morais-Cabral JH. Molecular Insights into the Mechanism of Calmodulin Inhibition of the EAG1 Potassium Channel. Structure. 2016 Sep 7. pii: S0969-2126(16)30234-9. doi:, 10.1016/j.str.2016.07.020. PMID:27618660 doi:http://dx.doi.org/10.1016/j.str.2016.07.020
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