4e50 - Revision history

OCA at 08:49, 20 March 2024

2024-03-20T08:49:08Z

← Older revision		Revision as of 08:49, 20 March 2024
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	== Structural highlights ==		== 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>		<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='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>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.7Å</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>		</table>
	== Function ==		== 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>		[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 ==~~
	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<ref>PMID:23462742</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div~~>

	==See Also==		==See Also==

OCA at 06:50, 28 September 2022

2022-09-28T06:50:18Z

← Older revision		Revision as of 06:50, 28 September 2022
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	<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== 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>		</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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[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~~]]

OCA at 17:45, 14 August 2019

2019-08-14T17:45:49Z

← Older revision		Revision as of 17:45, 14 August 2019
Line 1:		Line 1:

	==Calmodulin and Ng peptide complex==		==Calmodulin and Ng peptide complex==
	<StructureSection load='4e50' size='340' side='right' caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4e50' size='340' side='right'caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== 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. 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>
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	</div>		</div>
	<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Large Structures]]
	[[Category: Kumar, V]]		[[Category: Kumar, V]]
	[[Category: Sivaraman, J]]		[[Category: Sivaraman, J]]

OCA at 12:35, 6 November 2017

2017-11-06T12:35:45Z

← Older revision		Revision as of 12:35, 6 November 2017
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	</div>		</div>
	<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div>

	~~==See Also==~~
	*[[Calmodulin\|Calmodulin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 10:20, 3 August 2017

2017-08-03T10:20:51Z

← Older revision		Revision as of 10:20, 3 August 2017
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	<StructureSection load='4e50' size='340' side='right' caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4e50' size='340' side='right' caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e50]] is a 1 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=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. 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>
	</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e53\|4e53]]</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>		<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>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	~~[[Category: Lk3 transgenic mice]]~~
	[[Category: Kumar, V]]		[[Category: Kumar, V]]
	[[Category: Sivaraman, J]]		[[Category: Sivaraman, J]]

OCA at 13:23, 11 August 2016

2016-08-11T13:23:00Z

← Older revision		Revision as of 13:23, 11 August 2016
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	==Calmodulin and Ng peptide complex==		==Calmodulin and Ng peptide complex==
	<StructureSection load='4e50' size='340' side='right' caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>		<StructureSection load='4e50' size='340' side='right' caption='[[4e50]], [[Resolution\|resolution]] 2.70Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4e50]] is a 1 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=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 [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=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>
	</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e53\|4e53]]</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://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [http://www.ebi.ac.uk/pdbsum/4e50 PDBsum]</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>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 4e50" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 13:39, 4 January 2015

2015-01-04T13:39:27Z

← Older revision		Revision as of 13:39, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e50]] is a 1 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=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 [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=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>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e53\|4e53]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4e53\|4e53]]</td></tr>
	<tr><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://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [http://www.ebi.ac.uk/pdbsum/4e50 PDBsum]</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://www.rcsb.org/pdb/explore.do?structureId=4e50 RCSB], [http://www.ebi.ac.uk/pdbsum/4e50 PDBsum]</span></td></tr>
	<table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	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<ref>PMID:23462742</ref>		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<ref>PMID:23462742</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>

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	</StructureSection>		</StructureSection>
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Kumar, V.]]		[[Category: Kumar, V]]
	[[Category: Sivaraman, J.]]		[[Category: Sivaraman, J]]
	[[Category: Intrinsically unstructured protein]]		[[Category: Intrinsically unstructured protein]]
	[[Category: Iq motif]]		[[Category: Iq motif]]
	[[Category: Neurogranin]]		[[Category: Neurogranin]]
	[[Category: Protein binding]]		[[Category: Protein binding]]

OCA at 07:20, 5 June 2014

2014-06-05T07:20:36Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Calmodulin and Ng peptide complex==
-The entry 4e50 is ON HOLD  until Paper Publication
+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<ref>PMID:23462742</ref>
-Authors: Kumar, V., Sivaraman, J.
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-Description: Calmodulin and Ng peptide complex
+==See Also==

OCA at 08:50, 25 April 2012

2012-04-25T08:50:56Z

← Older revision		Revision as of 08:50, 25 April 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e50 is ON HOLD		The entry 4e50 is ON HOLD until Paper Publication

	Authors: Kumar, V., Sivaraman, J.		Authors: Kumar, V., Sivaraman, J.

	Description: Calmodulin and Ng peptide complex		Description: Calmodulin and Ng peptide complex

OCA at 07:22, 28 March 2012

2012-03-28T07:22:01Z

← Older revision		Revision as of 07:22, 28 March 2012
Line 3:		Line 3:
	The entry 4e50 is ON HOLD		The entry 4e50 is ON HOLD

	Authors: ~~Veerendra~~ Kumar, ~~Jayaraman~~ Sivaraman		Authors: Kumar, V., Sivaraman, J.

	Description: Calmodulin and Ng peptide complex		Description: Calmodulin and Ng peptide complex