7siz
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==C-type inactivation in a voltage gated K+ channel== | |
| + | <StructureSection load='7siz' size='340' side='right'caption='[[7siz]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7siz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SIZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SIZ 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]] 3.1Å</td></tr> | ||
| + | <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></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=7siz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7siz OCA], [https://pdbe.org/7siz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7siz RCSB], [https://www.ebi.ac.uk/pdbsum/7siz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7siz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == 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 is a process by which ion flux through a voltage-gated K(+) (K(v)) channel is regulated at the selectivity filter. While prior studies have indicated that C-type inactivation involves structural changes at the selectivity filter, the nature of the changes has not been resolved. Here, we report the crystal structure of the K(v)1.2 channel in a C-type inactivated state. The structure shows that C-type inactivation involves changes in the selectivity filter that disrupt the outer two ion binding sites in the filter. The changes at the selectivity filter propagate to the extracellular mouth and the turret regions of the channel pore. The structural changes observed are consistent with the functional hallmarks of C-type inactivation. This study highlights the intricate interplay between K(+) occupancy at the ion binding sites and the interactions of the selectivity filter in determining the balance between the conductive and the inactivated conformations of the filter. | ||
| - | + | Structural basis for C-type inactivation in a Shaker family voltage-gated K(+) channel.,Reddi R, Matulef K, Riederer EA, Whorton MR, Valiyaveetil FI Sci Adv. 2022 Apr 22;8(16):eabm8804. doi: 10.1126/sciadv.abm8804. Epub 2022 Apr , 22. PMID:35452285<ref>PMID:35452285</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7siz" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Potassium channel 3D structures|Potassium channel 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rattus norvegicus]] | ||
| + | [[Category: Matulef K]] | ||
| + | [[Category: Reddi R]] | ||
| + | [[Category: Riederer EA]] | ||
| + | [[Category: Valiyaveetil FI]] | ||
| + | [[Category: Whorton MR]] | ||
Current revision
C-type inactivation in a voltage gated K+ channel
| |||||||||||
