8j7h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:28, 15 January 2025) (edit) (undo)
 
Line 7: Line 7:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8j7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j7h OCA], [https://pdbe.org/8j7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j7h RCSB], [https://www.ebi.ac.uk/pdbsum/8j7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j7h 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=8j7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j7h OCA], [https://pdbe.org/8j7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j7h RCSB], [https://www.ebi.ac.uk/pdbsum/8j7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j7h ProSAT]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/R1FVI4_EMIHU R1FVI4_EMIHU] [https://www.uniprot.org/uniprot/R1EKX3_EMIHU R1EKX3_EMIHU] [https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Voltage-gated sodium (Na(V)) channels mediate a plethora of electrical activities. Na(V) channels govern cellular excitability in response to depolarizing stimuli. Inactivation is an intrinsic property of Na(V) channels that regulates cellular excitability by controlling the channel availability. The fast inactivation, mediated by the Ile-Phe-Met (IFM) motif and the N-terminal helix (N-helix), has been well-characterized. However, the molecular mechanism underlying Na(V) channel slow inactivation remains elusive. Here, we demonstrate that the removal of the N-helix of Na(V)Eh (Na(V)Eh(DeltaN)) results in a slow-inactivated channel, and present cryo-EM structure of Na(V)Eh(DeltaN) in a potential slow-inactivated state. The structure features a closed activation gate and a dilated selectivity filter (SF), indicating that the upper SF and the inner gate could serve as a gate for slow inactivation. In comparison to the Na(V)Eh structure, Na(V)Eh(DeltaN) undergoes marked conformational shifts on the intracellular side. Together, our results provide important mechanistic insights into Na(V) channel slow inactivation.
 +
 +
Structural mechanism of voltage-gated sodium channel slow inactivation.,Chen H, Xia Z, Dong J, Huang B, Zhang J, Zhou F, Yan R, Shi Y, Gong J, Jiang J, Huang Z, Jiang D Nat Commun. 2024 May 1;15(1):3691. doi: 10.1038/s41467-024-48125-3. PMID:38693179<ref>PMID:38693179</ref>
 +
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 8j7h" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
Line 12: Line 25:
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen HW]]
[[Category: Chen HW]]
-
[[Category: Jiang DH]]
+
[[Category: Jiang D]]

Current revision

ion channel

PDB ID 8j7h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools