3k6n

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain

Structural highlights

3k6n is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KCNJ3_MOUSE This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Strong voltage sensitivity of inward-rectifier K(+) (Kir) channels has been hypothesized to arise primarily from an intracellular blocker displacing up to five K(+) ions from the wide, intracellular part of the ion conduction pore outwardly across the narrow ion-selectivity filter. The validity of this hypothesis depends on two assumptions: (i) that five ion sites are located intracellular to the filter and (ii) that the blocker can force essentially unidirectional K(+) movement in a pore region generally wider than the combined dimensions of the blocker plus a K(+) ion. Here we present a crystal structure of the cytoplasmic portion of a Kir channel with five ions bound and demonstrate that a constriction near the intracellular end of the pore, acting as a gasket, prevents K(+) ions from bypassing the blocker. This heretofore unrecognized 'gasket' ensures that the blocker can effectively displace K(+) ions across the selectivity filter to generate exceedingly strong voltage sensitivity.

Physical determinants of strong voltage sensitivity of K(+) channel block.,Xu Y, Shin HG, Szep S, Lu Z Nat Struct Mol Biol. 2009 Dec;16(12):1252-8. Epub 2009 Nov 15. PMID:19915587^[1]

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

References

↑ Xu Y, Shin HG, Szep S, Lu Z. Physical determinants of strong voltage sensitivity of K(+) channel block. Nat Struct Mol Biol. 2009 Dec;16(12):1252-8. Epub 2009 Nov 15. PMID:19915587 doi:10.1038/nsmb.1717

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k6n"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain==
-<StructureSection load='3k6n' size='340' side='right' caption='[[3k6n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3k6n' size='340' side='right'caption='[[3k6n]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3k6n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K6N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3k6n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n9p|1n9p]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Girk1, Kcnj3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3k6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6n OCA], [https://pdbe.org/3k6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6n RCSB], [https://www.ebi.ac.uk/pdbsum/3k6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6n ProSAT]</span></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=3k6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6n OCA], [http://pdbe.org/3k6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6n RCSB], [http://www.ebi.ac.uk/pdbsum/3k6n PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/IRK3_MOUSE IRK3_MOUSE]] This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
+[https://www.uniprot.org/uniprot/KCNJ3_MOUSE KCNJ3_MOUSE] This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k6n_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k6/3k6n_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Potassium Channel|Potassium Channel]]
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Lu, Z]]
+[[Category: Mus musculus]]
-[[Category: Shin, H G]]
+[[Category: Lu Z]]
-[[Category: Szep, S]]
+[[Category: Shin HG]]
-[[Category: Xu, Y]]
+[[Category: Szep S]]
-[[Category: Beta barrel]]
+[[Category: Xu Y]]
-[[Category: Cytoplasmic domain]]
-[[Category: G protein]]
-[[Category: Inward rectifier]]
-[[Category: Ion transport]]
-[[Category: Ionic channel]]
-[[Category: Metal transport]]
-[[Category: Potassium channel]]
-[[Category: Transmembrane]]

3k6n

From Proteopedia

Current revision

Crystal structure of the S225E mutant Kir3.1 cytoplasmic pore domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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