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4ekw

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Revision as of 07:15, 28 September 2022

Crystal structure of the NavAb voltage-gated sodium channel (wild-type, 3.2 A)

Structural highlights

4ekw is a 4 chain structure with sequence from Aliarcobacter butzleri RM4018. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[A8EVM5_ALIB4]

Publication Abstract from PubMed

In excitable cells, voltage-gated sodium (Na(V)) channels activate to initiate action potentials and then undergo fast and slow inactivation processes that terminate their ionic conductance. Inactivation is a hallmark of Na(V) channel function and is critical for control of membrane excitability, but the structural basis for this process has remained elusive. Here we report crystallographic snapshots of the wild-type Na(V)Ab channel from Arcobacter butzleri captured in two potentially inactivated states at 3.2 A resolution. Compared to previous structures of Na(V)Ab channels with cysteine mutations in the pore-lining S6 helices (ref. 4), the S6 helices and the intracellular activation gate have undergone significant rearrangements: one pair of S6 helices has collapsed towards the central pore axis and the other S6 pair has moved outward to produce a striking dimer-of-dimers configuration. An increase in global structural asymmetry is observed throughout our wild-type Na(V)Ab models, reshaping the ion selectivity filter at the extracellular end of the pore, the central cavity and its residues that are analogous to the mammalian drug receptor site, and the lateral pore fenestrations. The voltage-sensing domains have also shifted around the perimeter of the pore module in wild-type Na(V)Ab, compared to the mutant channel, and local structural changes identify a conserved interaction network that connects distant molecular determinants involved in Na(V) channel gating and inactivation. These potential inactivated-state structures provide new insights into Na(V) channel gating and novel avenues to drug development and therapy for a range of debilitating Na(V) channelopathies.

Crystal structure of a voltage-gated sodium channel in two potentially inactivated states.,Payandeh J, Gamal El-Din TM, Scheuer T, Zheng N, Catterall WA Nature. 2012 May 20;486(7401):135-9. doi: 10.1038/nature11077. PMID:22678296^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Payandeh J, Gamal El-Din TM, Scheuer T, Zheng N, Catterall WA. Crystal structure of a voltage-gated sodium channel in two potentially inactivated states. Nature. 2012 May 20;486(7401):135-9. doi: 10.1038/nature11077. PMID:22678296 doi:http://dx.doi.org/10.1038/nature11077

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ekw"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the NavAb voltage-gated sodium channel (wild-type, 3.2 A)==
-<StructureSection load='4ekw' size='340' side='right' caption='[[4ekw]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
+<StructureSection load='4ekw' size='340' side='right'caption='[[4ekw]], [[Resolution|resolution]] 3.21&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ekw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcb4 Arcb4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EKW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ekw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aliarcobacter_butzleri_RM4018 Aliarcobacter butzleri RM4018]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EKW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PX4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PX4</scene></td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4ekw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekw OCA], [https://pdbe.org/4ekw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ekw RCSB], [https://www.ebi.ac.uk/pdbsum/4ekw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ekw ProSAT]</span></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rvy|3rvy]], [[3rvz|3rvz]], [[3rw0|3rw0]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Abu_1752 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=367737 ARCB4])</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=4ekw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ekw OCA], [http://pdbe.org/4ekw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ekw RCSB], [http://www.ebi.ac.uk/pdbsum/4ekw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ekw ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[https://www.uniprot.org/uniprot/A8EVM5_ALIB4 A8EVM5_ALIB4]]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 18: @@
 </div>
 <div class="pdbe-citations 4ekw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ion channels 3D structures|Ion channels 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Arcb4]]
+[[Category: Aliarcobacter butzleri RM4018]]
-[[Category: Catterall, W A]]
+[[Category: Large Structures]]
-[[Category: El-Din, T M.Gamal]]
+[[Category: Catterall WA]]
-[[Category: Payandeh, J]]
+[[Category: Gamal El-Din TM]]
-[[Category: Scheuer, T]]
+[[Category: Payandeh J]]
-[[Category: Zheng, N]]
+[[Category: Scheuer T]]
-[[Category: Membrane]]
+[[Category: Zheng N]]
-[[Category: Tetrameric ion channel superfamily]]
-[[Category: Transport protein]]
-[[Category: Voltage-gated ion channel]]
-[[Category: Voltage-gated sodium channel]]

4ekw

From Proteopedia

Revision as of 07:15, 28 September 2022

Crystal structure of the NavAb voltage-gated sodium channel (wild-type, 3.2 A)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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