2k0g: Difference between revisions
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<StructureSection load='2k0g' size='340' side='right'caption='[[2k0g]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | <StructureSection load='2k0g' size='340' side='right'caption='[[2k0g]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k0g]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2k0g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_loti Rhizobium loti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K0G FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0g OCA], [https://pdbe.org/2k0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k0g RCSB], [https://www.ebi.ac.uk/pdbsum/2k0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:30, 27 January 2022
Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMPSolution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMP
Structural highlights
Function[CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.[1] 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 PubMedCyclic nucleotide-sensitive ion channels, known as HCN and CNG channels, are crucial in neuronal excitability and signal transduction of sensory cells. HCN and CNG channels are activated by binding of cyclic nucleotides to their intracellular cyclic nucleotide-binding domain (CNBD). However, the mechanism by which the binding of cyclic nucleotides opens these channels is not well understood. Here, we report the solution structure of the isolated CNBD of a cyclic nucleotide-sensitive K(+) channel from Mesorhizobium loti. The protein consists of a wide anti-parallel beta-roll topped by a helical bundle comprising five alpha-helices and a short 3(10)-helix. In contrast to the dimeric arrangement ('dimer-of-dimers') in the crystal structure, the solution structure clearly shows a monomeric fold. The monomeric structure of the CNBD supports the hypothesis that the CNBDs transmit the binding signal to the channel pore independently of each other. Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP.,Schunke S, Stoldt M, Novak K, Kaupp UB, Willbold D EMBO Rep. 2009 Jul;10(7):729-35. Epub 2009 May 22. PMID:19465888[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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