2a79: Difference between revisions
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<StructureSection load='2a79' size='340' side='right'caption='[[2a79]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='2a79' size='340' side='right'caption='[[2a79]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a79]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2a79]] 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=2A79 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A79 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id=' | <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=2a79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a79 OCA], [https://pdbe.org/2a79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a79 RCSB], [https://www.ebi.ac.uk/pdbsum/2a79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a79 ProSAT]</span></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=2a79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a79 OCA], [https://pdbe.org/2a79 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a79 RCSB], [https://www.ebi.ac.uk/pdbsum/2a79 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a79 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: Campbell EB]] | ||
[[Category: | [[Category: Long SB]] | ||
[[Category: | [[Category: MacKinnon R]] | ||
Latest revision as of 10:20, 23 August 2023
Mammalian Shaker Kv1.2 potassium channel- beta subunit complexMammalian Shaker Kv1.2 potassium channel- beta subunit complex
Structural highlights
FunctionKCAB2_RAT Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. 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 PubMedVoltage-dependent potassium ion (K+) channels (Kv channels) conduct K+ ions across the cell membrane in response to changes in the membrane voltage, thereby regulating neuronal excitability by modulating the shape and frequency of action potentials. Here we report the crystal structure, at a resolution of 2.9 angstroms, of a mammalian Kv channel, Kv1.2, which is a member of the Shaker K+ channel family. This structure is in complex with an oxido-reductase beta subunit of the kind that can regulate mammalian Kv channels in their native cell environment. The activation gate of the pore is open. Large side portals communicate between the pore and the cytoplasm. Electrostatic properties of the side portals and positions of the T1 domain and beta subunit are consistent with electrophysiological studies of inactivation gating and with the possibility of K+ channel regulation by the beta subunit. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel.,Long SB, Campbell EB, Mackinnon R Science. 2005 Aug 5;309(5736):897-903. Epub 2005 Jul 7. PMID:16002581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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