5wie: Difference between revisions
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New page: ==Crystal structure of a Kv1.2-2.1 chimera K+ channel V406W mutant in an inactivated state== <StructureSection load='5wie' size='340' side='right' caption='5wie, [[Resolution|resoluti... |
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==Crystal structure of a Kv1.2-2.1 chimera K+ channel V406W mutant in an inactivated state== | ==Crystal structure of a Kv1.2-2.1 chimera K+ channel V406W mutant in an inactivated state== | ||
<StructureSection load='5wie' size='340' side='right' caption='[[5wie]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='5wie' size='340' side='right'caption='[[5wie]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5wie]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WIE OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5wie]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=5WIE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WIE FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</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]] 3.3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</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=5wie FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wie OCA], [https://pdbe.org/5wie PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wie RCSB], [https://www.ebi.ac.uk/pdbsum/5wie PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wie ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
C-type inactivation underlies important roles played by voltage-gated K+ (Kv) channels. Functional studies have provided strong evidence that a common underlying cause of this type of inactivation is an alteration near the extracellular end of the channel's ion-selectivity filter. Unlike N-type inactivation, which is known to reflect occlusion of the channel's intracellular end, the structural mechanism of C-type inactivation remains controversial and may have many detailed variations. Here we report that in voltage-gated Shaker K+ channels lacking N-type inactivation, a mutation enhancing inactivation disrupts the outermost K+ site in the selectivity filter. Furthermore, in a crystal structure of the Kv1.2-2.1 chimeric channel bearing the same mutation, the outermost K+ site, which is formed by eight carbonyl-oxygen atoms, appears to be slightly too small to readily accommodate a K+ ion and in fact exhibits little ion density; this structural finding is consistent with the functional hallmark of C-type inactivation. | |||
Crystal structure of an inactivated mutant mammalian voltage-gated K+ channel.,Pau V, Zhou Y, Ramu Y, Xu Y, Lu Z Nat Struct Mol Biol. 2017 Aug 28. doi: 10.1038/nsmb.3457. PMID:28846092<ref>PMID:28846092</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5wie" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Potassium channel 3D structures|Potassium channel 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Lu Z]] | ||
[[Category: | [[Category: Pau V]] | ||
[[Category: | [[Category: Ramu Y]] | ||
[[Category: | [[Category: Xu Y]] | ||
[[Category: | [[Category: Zhou Y]] | ||
Latest revision as of 14:13, 4 October 2023
Crystal structure of a Kv1.2-2.1 chimera K+ channel V406W mutant in an inactivated state
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