8ep1: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8ep1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EP1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[8ep1]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EP1 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=8ep1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ep1 OCA], [https://pdbe.org/8ep1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ep1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ep1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ep1 ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 5.4&#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=8ep1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ep1 OCA], [https://pdbe.org/8ep1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ep1 RCSB], [https://www.ebi.ac.uk/pdbsum/8ep1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ep1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/KCNH1_RAT KCNH1_RAT] Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). Mediates IK(NI) current in myoblasts (By similarity). Involved in the regulation of cell proliferation and differentiation, as adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity).[UniProtKB:O95259][UniProtKB:Q60603]
[https://www.uniprot.org/uniprot/KCNH1_RAT KCNH1_RAT] Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel. Channel properties may be modulated by subunit assembly, but not by cyclic nucleotides (By similarity). Mediates IK(NI) current in myoblasts (By similarity). Involved in the regulation of cell proliferation and differentiation, as adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity).[UniProtKB:O95259][UniProtKB:Q60603]
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== Publication Abstract from PubMed ==
Voltage-dependent ion channels regulate the opening of their pores by sensing the membrane voltage. This process underlies the propagation of action potentials and other forms of electrical activity in cells. The voltage dependence of these channels is governed by the transmembrane displacement of the positive charged S4 helix within their voltage-sensor domains. We use cryo-electron microscopy to visualize this movement in the mammalian Eag voltage-dependent potassium channel in lipid membrane vesicles with a voltage difference across the membrane. Multiple structural configurations show that the applied electric field displaces S4 toward the cytoplasm by two helical turns, resulting in an extended interfacial helix near the inner membrane leaflet. The position of S4 in this down conformation is sterically incompatible with an open pore, thus explaining how movement of the voltage sensor at hyperpolarizing membrane voltages locks the pore shut in this kind of voltage-dependent K&lt;sup&gt;+&lt;/sup&gt; (K&lt;sub&gt;v&lt;/sub&gt;) channel. The structures solved in lipid bilayer vesicles detail the intricate interplay between K&lt;sub&gt;v&lt;/sub&gt; channels and membranes, from showing how arginines are stabilized deep within the membrane and near phospholipid headgroups, to demonstrating how the channel reshapes the inner leaflet of the membrane itself.


Voltage-sensor movements in the Eag Kv channel under an applied electric field.,Mandala VS, MacKinnon R Proc Natl Acad Sci U S A. 2022 Nov 16;119(46):e2214151119. doi:, 10.1073/pnas.2214151119. Epub 2022 Nov 7. PMID:36331999<ref>PMID:36331999</ref>
==See Also==
 
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8ep1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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Latest revision as of 06:37, 19 June 2024

Eag Kv channel with voltage sensor in the down conformation

8ep1, resolution 5.40Å

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