6rv2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 6rv2 is ON HOLD until Paper Publication
==Crystal structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1) in a closed conformation==
 
<StructureSection load='6rv2' size='340' side='right'caption='[[6rv2]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6rv2]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RV2 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMU:DECYL-BETA-D-MALTOPYRANOSIDE'>DMU</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PC1:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PC1</scene>, <scene name='pdbligand=Y01:CHOLESTEROL+HEMISUCCINATE'>Y01</scene></td></tr>
[[Category: Unreleased Structures]]
<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=6rv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rv2 OCA], [http://pdbe.org/6rv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rv2 RCSB], [http://www.ebi.ac.uk/pdbsum/6rv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rv2 ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://www.uniprot.org/uniprot/KCNK3_HUMAN KCNK3_HUMAN]] Heritable pulmonary arterial hypertension. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
[[http://www.uniprot.org/uniprot/KCNK3_HUMAN KCNK3_HUMAN]] pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.<ref>PMID:23169818</ref> <ref>PMID:9312005</ref>  
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Arrowsmith, C H]]
[[Category: Bountra, C]]
[[Category: Burgess-Brown, N]]
[[Category: Bushell, S R]]
[[Category: Carpenter, E P]]
[[Category: Chalk, R]]
[[Category: Edwards, A M]]
[[Category: Mukhopadhyay, S M.M]]
[[Category: Pike, A C.W]]
[[Category: Quigley, A]]
[[Category: Rodstrom, K E.J]]
[[Category: Structural genomic]]
[[Category: Shrestha, L]]
[[Category: Speedman, D]]
[[Category: Tessitore, A]]
[[Category: Venkaya, S]]
[[Category: Zhang, W]]
[[Category: Membrane protein]]
[[Category: Potassium channel]]
[[Category: Sgc]]

Revision as of 09:06, 7 August 2019

Crystal structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1) in a closed conformationCrystal structure of the human two pore domain potassium ion channel TASK-1 (K2P3.1) in a closed conformation

Structural highlights

6rv2 is a 4 chain structure. 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

Disease

[KCNK3_HUMAN] Heritable pulmonary arterial hypertension. The disease is caused by mutations affecting the gene represented in this entry.

Function

[KCNK3_HUMAN] pH-dependent, voltage-insensitive, background potassium channel protein. Rectification direction results from potassium ion concentration on either side of the membrane. Acts as an outward rectifier when external potassium concentration is low. When external potassium concentration is high, current is inward.[1] [2]

References

  1. Plant LD, Zuniga L, Araki D, Marks JD, Goldstein SA. SUMOylation silences heterodimeric TASK potassium channels containing K2P1 subunits in cerebellar granule neurons. Sci Signal. 2012 Nov 20;5(251):ra84. doi: 10.1126/scisignal.2003431. PMID:23169818 doi:http://dx.doi.org/10.1126/scisignal.2003431
  2. Duprat F, Lesage F, Fink M, Reyes R, Heurteaux C, Lazdunski M. TASK, a human background K+ channel to sense external pH variations near physiological pH. EMBO J. 1997 Sep 1;16(17):5464-71. doi: 10.1093/emboj/16.17.5464. PMID:9312005 doi:http://dx.doi.org/10.1093/emboj/16.17.5464

6rv2, resolution 3.00Å

Drag the structure with the mouse to rotate

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

OCA