4hex

From Proteopedia

(Difference between revisions)

Revision as of 08:13, 3 November 2022

A novel conformation of calmodulin

Structural highlights

4hex is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]

Publication Abstract from PubMed

Calmodulin (CaM) is a highly conserved eukaryotic protein that binds specifically to more than 100 target proteins in response to calcium (Ca(2+)) signal. CaM adopts a considerable degree of structural plasticity to accomplish this physiological role; however, the nature and extent of this plasticity remain to be fully understood. Here, we report the crystal structure of a novel trans conformation of ligand-free CaM where the relative disposition of two lobes of CaM is different, a conformation to-date not reported. While no major structural changes were observed in the independent N- and C-lobes as compared with previously reported structures of Ca(2+)/CaM, the central helix was tilted by approximately 90 degrees at Arg75. This is the first crystal structure of CaM to show a drastic conformational change in the central helix, and reveals one of several possible conformations of CaM to engage with its binding partner.

A novel trans conformation of ligand-free calmodulin.,Kumar V, Chichili VP, Tang X, Sivaraman J PLoS One. 2013;8(1):e54834. doi: 10.1371/journal.pone.0054834. Epub 2013 Jan 29. PMID:23382982^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kumar V, Chichili VP, Tang X, Sivaraman J. A novel trans conformation of ligand-free calmodulin. PLoS One. 2013;8(1):e54834. doi: 10.1371/journal.pone.0054834. Epub 2013 Jan 29. PMID:23382982 doi:http://dx.doi.org/10.1371/journal.pone.0054834

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4hex"

Categories: Large Structures | Mus musculus | Chichili VPR | Kumar V | Sivaraman J

@@ Line 1: / Line 1: @@
 ==A novel conformation of calmodulin==
-<StructureSection load='4hex' size='340' side='right' caption='[[4hex]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='4hex' size='340' side='right'caption='[[4hex]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4hex]] is a 2 chain structure with sequence from [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=4HEX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HEX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4hex]] 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=4HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HEX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [https://pdbe.org/4hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [https://www.ebi.ac.uk/pdbsum/4hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex 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=4hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hex OCA], [http://pdbe.org/4hex PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hex RCSB], [http://www.ebi.ac.uk/pdbsum/4hex PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hex 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]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 </div>
 <div class="pdbe-citations 4hex" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Chichili, V P.R]]
+[[Category: Mus musculus]]
-[[Category: Kumar, V]]
+[[Category: Chichili VPR]]
-[[Category: Sivaraman, J]]
+[[Category: Kumar V]]
-[[Category: Calcium binding]]
+[[Category: Sivaraman J]]
-[[Category: Calcium binding protein]]
-[[Category: Calcium signalling]]
-[[Category: Calmodulin]]
-[[Category: Ef-hand motif]]
-[[Category: Neurogranin]]
-[[Category: Neuromodulin]]
-[[Category: Novel conformation]]
-[[Category: Tran]]

4hex

From Proteopedia

Revision as of 08:13, 3 November 2022

A novel conformation of calmodulin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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