7phi: Difference between revisions

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<StructureSection load='7phi' size='340' side='right'caption='[[7phi]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='7phi' size='340' side='right'caption='[[7phi]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7phi]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PHI FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PHI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PCF:1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE'>PCF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PCF:1,2-DIACYL-SN-GLYCERO-3-PHOSHOCHOLINE'>PCF</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7phi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7phi OCA], [https://pdbe.org/7phi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7phi RCSB], [https://www.ebi.ac.uk/pdbsum/7phi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7phi 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=7phi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7phi OCA], [https://pdbe.org/7phi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7phi RCSB], [https://www.ebi.ac.uk/pdbsum/7phi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7phi ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kv3 channels have distinctive gating kinetics tailored for rapid repolarization in fast-spiking neurons. Malfunction of this process due to genetic variants in the KCNC1 gene causes severe epileptic disorders, yet the structural determinants for the unusual gating properties remain elusive. Here, we present cryo-electron microscopy structures of the human Kv3.1a channel, revealing a unique arrangement of the cytoplasmic tetramerization domain T1 which facilitates interactions with C-terminal axonal targeting motif and key components of the gating machinery. Additional interactions between S1/S2 linker and turret domain strengthen the interface between voltage sensor and pore domain. Supported by molecular dynamics simulations, electrophysiological and mutational analyses, we identify several residues in the S4/S5 linker which influence the gating kinetics and an electrostatic interaction between acidic residues in alpha6 of T1 and R449 in the pore-flanking S6T helices. These findings provide insights into gating control and disease mechanisms and may guide strategies for the design of pharmaceutical drugs targeting Kv3 channels.


Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain.,Chi G, Liang Q, Sridhar A, Cowgill JB, Sader K, Radjainia M, Qian P, Castro-Hartmann P, Venkaya S, Singh NK, McKinley G, Fernandez-Cid A, Mukhopadhyay SMM, Burgess-Brown NA, Delemotte L, Covarrubias M, Durr KL Nat Commun. 2022 Jul 15;13(1):4087. doi: 10.1038/s41467-022-29594-w. PMID:35840580<ref>PMID:35840580</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>
</div>
<div class="pdbe-citations 7phi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Burgess-Brown, N A]]
[[Category: Burgess-Brown NA]]
[[Category: Castro-Hartmann, P]]
[[Category: Castro-Hartmann P]]
[[Category: Chi, G]]
[[Category: Chi G]]
[[Category: Duerr, K L]]
[[Category: Duerr KL]]
[[Category: Fernandez-Cid, A]]
[[Category: Fernandez-Cid A]]
[[Category: MacLean, E M]]
[[Category: MacLean EM]]
[[Category: Marsden, B]]
[[Category: Marsden B]]
[[Category: McKinley, G]]
[[Category: McKinley G]]
[[Category: Mukhopadhyay, S M.M]]
[[Category: Mukhopadhyay SMM]]
[[Category: Pike, A C.W]]
[[Category: Pike ACW]]
[[Category: Qian, P]]
[[Category: Qian P]]
[[Category: Sader, K]]
[[Category: Sader K]]
[[Category: Singh, N K]]
[[Category: Singh NK]]
[[Category: Venkaya, S]]
[[Category: Venkaya S]]
[[Category: Channel]]
[[Category: Membrane protein]]
[[Category: Potassium channel]]
[[Category: Tetramer]]
[[Category: Transport protein]]
[[Category: Voltage-gated]]

Latest revision as of 15:33, 17 July 2024

Human voltage-gated potassium channel Kv3.1 (with Zn)Human voltage-gated potassium channel Kv3.1 (with Zn)

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.1Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

7phi, resolution 3.10Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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