4e50: Difference between revisions

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'''Unreleased structure'''


The entry 4e50 is ON HOLD
==Calmodulin and Ng peptide complex==
<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4e50]] is a 1 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=4E50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E50 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]] 2.7&#8491;</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=4e50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e50 OCA], [https://pdbe.org/4e50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [https://www.ebi.ac.uk/pdbsum/4e50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e50 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/NEUG_MOUSE NEUG_MOUSE] Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.<ref>PMID:11016969</ref>


Authors: Kumar, V., Sivaraman, J.
==See Also==
 
*[[Calmodulin 3D structures|Calmodulin 3D structures]]
Description: Calmodulin and Ng peptide complex
== References ==
<references/>
__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 Ng peptide complexCalmodulin and Ng peptide complex

Structural highlights

4e50 is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
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]NEUG_MOUSE Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.[1]

See Also

References

  1. Pak JH, Huang FL, Li J, Balschun D, Reymann KG, Chiang C, Westphal H, Huang KP. Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice. Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11232-7. PMID:11016969 doi:http://dx.doi.org/10.1073/pnas.210184697

4e50, resolution 2.70Å

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OCA