This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


8e0e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: '''Unreleased structure''' The entry 8e0e is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (10:16, 25 October 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 8e0e is ON HOLD
+
==nbF3:CaV beta subunit 2a complex==
 +
<StructureSection load='8e0e' size='340' side='right'caption='[[8e0e]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[8e0e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] 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=8E0E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E0E FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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=8e0e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e0e OCA], [https://pdbe.org/8e0e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e0e RCSB], [https://www.ebi.ac.uk/pdbsum/8e0e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e0e ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/A0A8I6AEJ4_RAT A0A8I6AEJ4_RAT] The beta subunit of voltage-dependent calcium channels contributes to the function of the calcium channel by increasing peak calcium current, shifting the voltage dependencies of activation and inactivation, modulating G protein inhibition and controlling the alpha-1 subunit membrane targeting.[ARBA:ARBA00002749]
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Ca(2+) influx through high-voltage-activated calcium channels (HVACCs) controls diverse cellular functions. A critical feature enabling a singular signal, Ca(2+) influx, to mediate disparate functions is diversity of HVACC pore-forming alpha(1) and auxiliary Ca(V)beta(1)-Ca(V)beta(4) subunits. Selective Ca(V)alpha(1) blockers have enabled deciphering their unique physiological roles. By contrast, the capacity to post-translationally inhibit HVACCs based on Ca(V)beta isoform is non-existent. Conventional gene knockout/shRNA approaches do not adequately address this deficit owing to subunit reshuffling and partially overlapping functions of Ca(V)beta isoforms. Here, we identify a nanobody (nb.E8) that selectively binds Ca(V)beta(1) SH3 domain and inhibits Ca(V)beta(1)-associated HVACCs by reducing channel surface density, decreasing open probability, and speeding inactivation. Functionalizing nb.E8 with Nedd4L HECT domain yielded Chisel-1 which eliminated current through Ca(V)beta(1)-reconstituted Ca(V)1/Ca(V)2 and native Ca(V)1.1 channels in skeletal muscle, strongly suppressed depolarization-evoked Ca(2+) influx and excitation-transcription coupling in hippocampal neurons, but was inert against Ca(V)beta(2)-associated Ca(V)1.2 in cardiomyocytes. The results introduce an original method for probing distinctive functions of ion channel auxiliary subunit isoforms, reveal additional dimensions of Ca(V)beta(1) signaling in neurons, and describe a genetically-encoded HVACC inhibitor with unique properties.
-
Authors:
+
Selective posttranslational inhibition of Ca(V)beta(1)-associated voltage-dependent calcium channels with a functionalized nanobody.,Morgenstern TJ, Nirwan N, Hernandez-Ochoa EO, Bibollet H, Choudhury P, Laloudakis YD, Ben Johny M, Bannister RA, Schneider MF, Minor DL Jr, Colecraft HM Nat Commun. 2022 Dec 9;13(1):7556. doi: 10.1038/s41467-022-35025-7. PMID:36494348<ref>PMID:36494348</ref>
-
Description:
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[Category: Unreleased Structures]]
+
</div>
 +
<div class="pdbe-citations 8e0e" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Ion channels 3D structures|Ion channels 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Lama glama]]
 +
[[Category: Large Structures]]
 +
[[Category: Rattus norvegicus]]
 +
[[Category: Minor DL]]
 +
[[Category: Nirwan N]]

Current revision

nbF3:CaV beta subunit 2a complex

PDB ID 8e0e

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools