4j9z - Revision history

OCA at 12:02, 1 March 2024

OCA — Fri, 01 Mar 2024 12:02:36 GMT

←Older revision		Revision as of 12:02, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>		<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.66Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [https://pdbe.org/4j9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [https://www.ebi.ac.uk/pdbsum/4j9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9z 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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [https://pdbe.org/4j9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [https://www.ebi.ac.uk/pdbsum/4j9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.		[https://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Most proteins, such as ion channels, form well-organized 3D structures to carry out their specific functions. A typical voltage-gated potassium channel subunit has six transmembrane segments (S1-S6) to form the voltage-sensing domain and the pore domain. Conformational changes of these domains result in opening of the channel pore. Intrinsically disordered (ID) proteins/peptides are considered equally important for the protein functions. However, it is difficult to explore the structural features underlying the functions of ID proteins/peptides by conventional methods, such as X-ray crystallography, because of the flexibility of their secondary structures. Unlike voltage-gated potassium channels, families of small- and intermediate-conductance Ca(2+)-activated potassium (SK/IK) channels with important roles in regulating membrane excitability are activated exclusively by Ca(2+)-bound calmodulin (CaM). Upon binding of Ca(2+) to CaM, a 2 x 2 structure forms between CaM and the CaM-binding domain. A channel fragment that connects S6 and the CaM-binding domain is not visible in the protein crystal structure, suggesting that this fragment is an ID fragment. Here we show that the conformation of the ID fragment in SK channels becomes readily identifiable in the presence of NS309, the most potent compound that potentiates the channel activities. This well-defined conformation of the ID fragment, stabilized by NS309, increases the channel open probability at a given Ca(2+) concentration. Our results demonstrate that the ID fragment, itself a target for drugs modulating SK channel activities, plays a unique role in coupling Ca(2+) sensing by CaM and mechanical opening of SK channels.
-
-	Unstructured to structured transition of an intrinsically disordered protein peptide in coupling Ca2+-sensing and SK channel activation.,Zhang M, Pascal JM, Zhang JF Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4828-33. doi:, 10.1073/pnas.1220253110. Epub 2013 Mar 4. PMID:23487779<ref>PMID:23487779</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4j9z" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]		*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
	*[[Potassium channel 3D structures\|Potassium channel 3D structures]]		*[[Potassium channel 3D structures\|Potassium channel 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:01, 24 November 2022

OCA — Thu, 24 Nov 2022 11:01:19 GMT

←Older revision		Revision as of 11:01, 24 November 2022
Line 1:		Line 1:

	==Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309==		==Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309==
-	<StructureSection load='4j9z' size='340' side='right' caption='[[4j9z]], [[Resolution\|resolution]] 1.66Å' scene=''>	+	<StructureSection load='4j9z' size='340' side='right'caption='[[4j9z]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4y\|1g4y]], [[4g27\|4g27]], [[4g28\|4g28]], [[3sjq\|3sjq]], [[4j9y\|4j9y]]</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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [https://pdbe.org/4j9z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [https://www.ebi.ac.uk/pdbsum/4j9z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9z ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kcnn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [~~http~~://pdbe.org/4j9z PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4j9z PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9z ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.	+	[https://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 20:

	==See Also==		==See Also==
-	*[[Calmodulin\|Calmodulin]]	+	*[[Calmodulin 3D structures\|Calmodulin 3D structures]]
-	*[[Potassium ~~Channel~~\|Potassium ~~Channel~~]]	+	*[[Potassium channel 3D structures\|Potassium channel 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Buffalo rat~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Pascal, J M~~]]	+	[[Category: Rattus norvegicus]]
-	[[Category: ~~Zhang, J F~~]]	+	[[Category: Pascal JM]]
-	[[Category: Zhang~~, M~~]]	+	[[Category: Zhang J-F]]
-	[[Category: ~~Calcium binding]]~~	+	[[Category: Zhang M]]
-	~~[[Category: Ef hand]]~~	+
-	~~[[Category: Sk2a channel fragment]]~~	+
-	~~[[Category: Transport protein-calcium binding complex~~]]	+

OCA at 08:31, 4 August 2016

OCA — Thu, 04 Aug 2016 08:31:34 GMT

←Older revision		Revision as of 08:31, 4 August 2016
Line 1:		Line 1:
		+
	==Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309==		==Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309==
	<StructureSection load='4j9z' size='340' side='right' caption='[[4j9z]], [[Resolution\|resolution]] 1.66Å' scene=''>		<StructureSection load='4j9z' size='340' side='right' caption='[[4j9z]], [[Resolution\|resolution]] 1.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Rattus_norvegicus Rattus norvegicus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4y\|1g4y]], [[4g27\|4g27]], [[4g28\|4g28]], [[3sjq\|3sjq]], [[4j9y\|4j9y]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4y\|1g4y]], [[4g27\|4g27]], [[4g28\|4g28]], [[3sjq\|3sjq]], [[4j9y\|4j9y]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kcnn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~]), Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 ~~Rattus norvegicus~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kcnn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [http://www.ebi.ac.uk/pdbsum/4j9z 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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [http://pdbe.org/4j9z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [http://www.ebi.ac.uk/pdbsum/4j9z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9z ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4j9z" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 26:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Rattus norvegicus~~]]	+	[[Category: Buffalo rat]]
	[[Category: Pascal, J M]]		[[Category: Pascal, J M]]
	[[Category: Zhang, J F]]		[[Category: Zhang, J F]]

OCA at 07:42, 24 December 2014

OCA — Wed, 24 Dec 2014 07:42:46 GMT

←Older revision		Revision as of 07:42, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4j9z\| PDB=4j9z \| SCENE= }}~~	+	==Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309==
-	===Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309===	+	<StructureSection load='4j9z' size='340' side='right' caption='[[4j9z]], [[Resolution\|resolution]] 1.66Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23487779}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4j9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J9Z FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1KP:(3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-INDOL-2-ONE'>1KP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1g4y\|1g4y]], [[4g27\|4g27]], [[4g28\|4g28]], [[3sjq\|3sjq]], [[4j9y\|4j9y]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">Kcnn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=4j9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j9z RCSB], [http://www.ebi.ac.uk/pdbsum/4j9z PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.		[[http://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Most proteins, such as ion channels, form well-organized 3D structures to carry out their specific functions. A typical voltage-gated potassium channel subunit has six transmembrane segments (S1-S6) to form the voltage-sensing domain and the pore domain. Conformational changes of these domains result in opening of the channel pore. Intrinsically disordered (ID) proteins/peptides are considered equally important for the protein functions. However, it is difficult to explore the structural features underlying the functions of ID proteins/peptides by conventional methods, such as X-ray crystallography, because of the flexibility of their secondary structures. Unlike voltage-gated potassium channels, families of small- and intermediate-conductance Ca(2+)-activated potassium (SK/IK) channels with important roles in regulating membrane excitability are activated exclusively by Ca(2+)-bound calmodulin (CaM). Upon binding of Ca(2+) to CaM, a 2 x 2 structure forms between CaM and the CaM-binding domain. A channel fragment that connects S6 and the CaM-binding domain is not visible in the protein crystal structure, suggesting that this fragment is an ID fragment. Here we show that the conformation of the ID fragment in SK channels becomes readily identifiable in the presence of NS309, the most potent compound that potentiates the channel activities. This well-defined conformation of the ID fragment, stabilized by NS309, increases the channel open probability at a given Ca(2+) concentration. Our results demonstrate that the ID fragment, itself a target for drugs modulating SK channel activities, plays a unique role in coupling Ca(2+) sensing by CaM and mechanical opening of SK channels.
		+
		+	Unstructured to structured transition of an intrinsically disordered protein peptide in coupling Ca2+-sensing and SK channel activation.,Zhang M, Pascal JM, Zhang JF Proc Natl Acad Sci U S A. 2013 Mar 19;110(12):4828-33. doi:, 10.1073/pnas.1220253110. Epub 2013 Mar 4. PMID:23487779<ref>PMID:23487779</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~4j9z~~]] ~~is a 2 chain structure with sequence from~~ [~~http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from~~ [~~http:~~//~~oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA].~~	+	*[[Calmodulin\|Calmodulin]]
		+	*[[Potassium Channel\|Potassium Channel]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Rattus norvegicus]]		[[Category: Rattus norvegicus]]
-	[[Category: Pascal, J M.]]	+	[[Category: Pascal, J M]]
-	[[Category: Zhang, J F.]]	+	[[Category: Zhang, J F]]
-	[[Category: Zhang, M.]]	+	[[Category: Zhang, M]]
	[[Category: Calcium binding]]		[[Category: Calcium binding]]
	[[Category: Ef hand]]		[[Category: Ef hand]]
	[[Category: Sk2a channel fragment]]		[[Category: Sk2a channel fragment]]
	[[Category: Transport protein-calcium binding complex]]		[[Category: Transport protein-calcium binding complex]]

OCA at 08:41, 27 March 2013

OCA — Wed, 27 Mar 2013 08:41:12 GMT

←Older revision		Revision as of 08:41, 27 March 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4j9z\| PDB=4j9z \| SCENE= }}
		+	===Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309===
		+	{{ABSTRACT_PUBMED_23487779}}

-	The ~~entry 4j9z~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/KCNN2_RAT KCNN2_RAT]] Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.

-	~~Authors~~: ~~Zhang, M~~., Pascal, J.M., Zhang, J.-F.	+	==About this Structure==
-		+	[[4j9z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9Z OCA].
-	~~Description~~: Calcium~~-calmodulin complexed with the calmodulin~~ binding ~~domain from a small conductance potassium~~ channel ~~splice variant and NS309~~	+	[[Category: Rattus norvegicus]]
		+	[[Category: Pascal, J M.]]
		+	[[Category: Zhang, J F.]]
		+	[[Category: Zhang, M.]]
		+	[[Category: Calcium binding]]
		+	[[Category: Ef hand]]
		+	[[Category: Sk2a channel fragment]]
		+	[[Category: Transport protein-calcium binding complex]]

OCA at 16:17, 20 March 2013

OCA — Wed, 20 Mar 2013 16:17:11 GMT

←Older revision		Revision as of 16:17, 20 March 2013
Line 3:		Line 3:
	The entry 4j9z is ON HOLD		The entry 4j9z is ON HOLD

-	Authors: Zhang, M., Pascal, J.M., Zhang, J.-f.	+	Authors: Zhang, M., Pascal, J.M., Zhang, J.-F.

	Description: Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309		Description: Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309

OCA: Protected "4j9z" [edit=sysop:move=sysop]

OCA — Wed, 27 Feb 2013 14:26:48 GMT

Protected "4j9z" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:26, 27 February 2013

OCA: New page: '''Unreleased structure''' The entry 4j9z is ON HOLD Authors: Zhang, M., Pascal, J.M., Zhang, J.-f. Description: Calcium-calmodulin complexed with the calmodulin binding domain from a ...

OCA — Wed, 27 Feb 2013 14:26:47 GMT

New page: '''Unreleased structure''' The entry 4j9z is ON HOLD Authors: Zhang, M., Pascal, J.M., Zhang, J.-f. Description: Calcium-calmodulin complexed with the calmodulin binding domain from a ...

New page

'''Unreleased structure'''

The entry 4j9z is ON HOLD

Authors: Zhang, M., Pascal, J.M., Zhang, J.-f.

Description: Calcium-calmodulin complexed with the calmodulin binding domain from a small conductance potassium channel splice variant and NS309