6ebm: Difference between revisions

Latest revision as of 17:40, 13 March 2024

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alphaThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

6ebm, resolution 4.00Å

Structural highlights

6ebm is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4Å
Experimental data:	Check
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCNB2_RAT Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells (PubMed:1550672). Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:1550672). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:20202934). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes (PubMed:9305895). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells (PubMed:1550672, PubMed:20202934).[UniProtKB:A6H8H5]^[1] ^[2] ^[3] KCNA2_RAT Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.^[4]

References

↑ Hwang PM, Glatt CE, Bredt DS, Yellen G, Snyder SH. A novel K+ channel with unique localizations in mammalian brain: molecular cloning and characterization. Neuron. 1992 Mar;8(3):473-81. PMID:1550672 doi:10.1016/0896-6273(92)90275-i
↑ Kihira Y, Hermanstyne TO, Misonou H. Formation of heteromeric Kv2 channels in mammalian brain neurons. J Biol Chem. 2010 May 14;285(20):15048-15055. PMID:20202934 doi:10.1074/jbc.M109.074260
↑ Salinas M, Duprat F, Heurteaux C, Hugnot JP, Lazdunski M. New modulatory alpha subunits for mammalian Shab K+ channels. J Biol Chem. 1997 Sep 26;272(39):24371-9. PMID:9305895 doi:10.1074/jbc.272.39.24371
↑ Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J. Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature. 1995 Aug 31;376(6543):737-45. PMID:7544443 doi:http://dx.doi.org/10.1038/376737a0

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OCA

[1] Hwang PM, Glatt CE, Bredt DS, Yellen G, Snyder SH. A novel K+ channel with unique localizations in mammalian brain: molecular cloning and characterization. Neuron. 1992 Mar;8(3):473-81. PMID:1550672 doi:10.1016/0896-6273(92)90275-i

[2] Kihira Y, Hermanstyne TO, Misonou H. Formation of heteromeric Kv2 channels in mammalian brain neurons. J Biol Chem. 2010 May 14;285(20):15048-15055. PMID:20202934 doi:10.1074/jbc.M109.074260

[3] Salinas M, Duprat F, Heurteaux C, Hugnot JP, Lazdunski M. New modulatory alpha subunits for mammalian Shab K+ channels. J Biol Chem. 1997 Sep 26;272(39):24371-9. PMID:9305895 doi:10.1074/jbc.272.39.24371

[4] Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J. Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature. 1995 Aug 31;376(6543):737-45. PMID:7544443 doi:http://dx.doi.org/10.1038/376737a0

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[2]

[3]

[4]

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6ebm is ON HOLD
+==The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha==
+<SX load='6ebm' size='340' side='right' viewer='molstar' caption='[[6ebm]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ebm]] is a 4 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=6EBM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EBM FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#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=6ebm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ebm OCA], [https://pdbe.org/6ebm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ebm RCSB], [https://www.ebi.ac.uk/pdbsum/6ebm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ebm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KCNB2_RAT KCNB2_RAT] Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain and smooth muscle cells (PubMed:1550672). Channels open or close in response to the voltage difference across the membrane, letting potassium ions pass in accordance with their electrochemical gradient. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization (PubMed:1550672). Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB1; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:20202934). Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNS1 and KCNS2, creating a functionally diverse range of channel complexes (PubMed:9305895). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Contributes to the delayed-rectifier voltage-gated potassium current in cortical pyramidal neurons and smooth muscle cells (PubMed:1550672, PubMed:20202934).[UniProtKB:A6H8H5]<ref>PMID:1550672</ref> <ref>PMID:20202934</ref> <ref>PMID:9305895</ref> [https://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</ref>
-Authors: Matthies, D., Bae, C., Fox, T., Bartesaghi, A., Subramaniam, S., Swartz, K.J.
+==See Also==
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
-Description: KV1.2-KV2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Swartz, K.J]]
+__TOC__
-[[Category: Subramaniam, S]]
+</SX>
-[[Category: Matthies, D]]
+[[Category: Large Structures]]
-[[Category: Bae, C]]
+[[Category: Rattus norvegicus]]
-[[Category: Fox, T]]
+[[Category: Bae C]]
-[[Category: Bartesaghi, A]]
+[[Category: Bartesaghi A]]
+[[Category: Fox T]]
+[[Category: Matthies D]]
+[[Category: Subramaniam S]]
+[[Category: Swartz KJ]]

6ebm: Difference between revisions

Latest revision as of 17:40, 13 March 2024

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alphaThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

Structural highlights

Function

See Also

References

Contents

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6ebm: Difference between revisions

Latest revision as of 17:40, 13 March 2024

The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alphaThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, transmembrane domain of subunit alpha

Structural highlights

Function

See Also

References

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