2k0g

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[[Image:2k0g.png|left|200px]]
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==Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMP==
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<StructureSection load='2k0g' size='340' side='right' caption='[[2k0g]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2k0g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K0G FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k0g RCSB], [http://www.ebi.ac.uk/pdbsum/2k0g PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/2k0g_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclic 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.
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{{STRUCTURE_2k0g| PDB=2k0g | SCENE= }}
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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<ref>PMID:19465888</ref>
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===Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMP===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_19465888}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2k0g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K0G OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019465888</ref><references group="xtra"/>
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[[Category: Mesorhizobium loti]]
[[Category: Mesorhizobium loti]]
[[Category: Schunke, S.]]
[[Category: Schunke, S.]]

Revision as of 10:20, 30 September 2014

Solution Structure of a Bacterial Cyclic Nucleotide-Activated K+ Channel Binding Domain in Complex with cAMP

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