6vtl

From Proteopedia

(Difference between revisions)

Current revision

Structure of an acid-sensing ion channel solubilized by styrene maleic acid and in a resting state at high pH

Structural highlights

6vtl is a 3 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.65Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ASIC1_CHICK Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).^[1]

Publication Abstract from PubMed

Acid-sensing ion channels (ASICs) are proton-gated members of the epithelial sodium channel/degenerin (ENaC/DEG) superfamily of ion channels and are expressed throughout the central and peripheral nervous systems. The homotrimeric splice variant ASIC1a has been implicated in nociception, fear memory, mood disorders and ischemia. Here, we extract full-length chicken ASIC1 (cASIC1) from cell membranes using styrene maleic acid (SMA) copolymer, elucidating structures of ASIC1 channels in both high pH resting and low pH desensitized conformations by single-particle cryo-electron microscopy (cryo-EM). The structures of resting and desensitized channels reveal a reentrant loop at the amino terminus of ASIC1 that includes the highly conserved 'His-Gly' (HG) motif. The reentrant loop lines the lower ion permeation pathway and buttresses the 'Gly-Ala-Ser' (GAS) constriction, thus providing a structural explanation for the role of the His-Gly dipeptide in the structure and function of ASICs.

The His-Gly motif of acid-sensing ion channels resides in a reentrant 'loop' implicated in gating and ion selectivity.,Yoder N, Gouaux E Elife. 2020 Jun 4;9. pii: 56527. doi: 10.7554/eLife.56527. PMID:32496192^[2]

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

References

↑ Coric T, Zheng D, Gerstein M, Canessa CM. Proton sensitivity of ASIC1 appeared with the rise of fishes by changes of residues in the region that follows TM1 in the ectodomain of the channel. J Physiol. 2005 Nov 1;568(Pt 3):725-35. Epub 2005 Jul 7. PMID:16002453 doi:http://dx.doi.org/jphysiol.2005.087734
↑ Yoder N, Gouaux E. The His-Gly motif of acid-sensing ion channels resides in a reentrant 'loop' implicated in gating and ion selectivity. Elife. 2020 Jun 4;9. pii: 56527. doi: 10.7554/eLife.56527. PMID:32496192 doi:http://dx.doi.org/10.7554/eLife.56527

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/6vtl"

Categories: Gallus gallus | Large Structures | Gouaux E | Yoder N

@@ Line 3: / Line 3: @@
 <StructureSection load='6vtl' size='340' side='right'caption='[[6vtl]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6vtl]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VTL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VTL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6vtl]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VTL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 3.65&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6vtk|6vtk]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ASIC1, ACCN2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</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=6vtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vtl OCA], [https://pdbe.org/6vtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vtl RCSB], [https://www.ebi.ac.uk/pdbsum/6vtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vtl ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vtl OCA], [http://pdbe.org/6vtl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vtl RCSB], [http://www.ebi.ac.uk/pdbsum/6vtl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vtl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ASIC1_CHICK ASIC1_CHICK]] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).<ref>PMID:16002453</ref>
+[https://www.uniprot.org/uniprot/ASIC1_CHICK ASIC1_CHICK] Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride (By similarity).<ref>PMID:16002453</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </div>
 <div class="pdbe-citations 6vtl" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ion channels 3D structures|Ion channels 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Gouaux, E]]
+[[Category: Gouaux E]]
-[[Category: Yoder, N]]
+[[Category: Yoder N]]
-[[Category: Acid-sensing ion channel]]
-[[Category: Asic]]
-[[Category: Asic1a]]
-[[Category: Ligand-gated ion channel]]
-[[Category: Membrane protein]]
-[[Category: Proton-gated ion channel]]
-[[Category: Transport protein]]

6vtl

From Proteopedia

Current revision

Structure of an acid-sensing ion channel solubilized by styrene maleic acid and in a resting state at high pH

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox