4e50

From Proteopedia

(Difference between revisions)

Revision as of 06:50, 28 September 2022

Calmodulin 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.
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]

Publication Abstract from PubMed

Neuromodulin (Nm) and neurogranin (Ng) are neuron-specific substrates of protein kinase C (PKC). Their interactions with Calmodulin (CaM) are crucial for learning and memory formation in neurons. Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM. These observations explain the mechanism by which PKC-induced Ser phosphorylation blocks the association of Nm/Ng with CaM and interrupts several learning- and memory-associated functions. Moreover, the present study identified Arg as a key CaM interacting residue from Nm/Ng. This residue is crucial for CaM-mediated function, as evidenced by the inability of the Ng mutant (Arg-to-Ala) to potentiate synaptic transmission in CA1 hippocampal neurons.

Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin.,Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J Sci Rep. 2013 Mar 6;3:1392. doi: 10.1038/srep01392. PMID:23462742^[2]

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

References

↑ 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
↑ Kumar V, Chichili VP, Zhong L, Tang X, Velazquez-Campoy A, Sheu FS, Seetharaman J, Gerges NZ, Sivaraman J. Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin. Sci Rep. 2013 Mar 6;3:1392. doi: 10.1038/srep01392. PMID:23462742 doi:http://dx.doi.org/10.1038/srep01392

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/4e50"

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

@@ Line 3: / Line 3: @@
 <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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E50 FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e53|4e53]]</td></tr>
+</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>
-<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=4e50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e50 OCA], [http://pdbe.org/4e50 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [http://www.ebi.ac.uk/pdbsum/4e50 PDBsum], [http://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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Kumar, V]]
+[[Category: Mus musculus]]
-[[Category: Sivaraman, J]]
+[[Category: Kumar V]]
-[[Category: Intrinsically unstructured protein]]
+[[Category: Sivaraman J]]
-[[Category: Iq motif]]
-[[Category: Neurogranin]]
-[[Category: Protein binding]]

4e50

From Proteopedia

Revision as of 06:50, 28 September 2022

Calmodulin and Ng peptide complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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