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2k0g

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Revision as of 07:30, 27 January 2022

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

Structural highlights

2k0g is a 1 chain structure with sequence from Rhizobium loti. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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.

References

↑ Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel. Cell. 2004 Nov 24;119(5):615-27. PMID:15550244 doi:10.1016/j.cell.2004.10.030
↑ Schunke S, Stoldt M, Novak K, Kaupp UB, Willbold D. Solution structure of the Mesorhizobium loti K1 channel cyclic nucleotide-binding domain in complex with cAMP. EMBO Rep. 2009 Jul;10(7):729-35. Epub 2009 May 22. PMID:19465888 doi:10.1038/embor.2009.68

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k0g"

@@ Line 3: / Line 3: @@
 <StructureSection load='2k0g' size='340' side='right'caption='[[2k0g]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k0g]] is a 1 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=2K0G FirstGlance]. <br>
+<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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2k0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k0g OCA], [http://pdbe.org/2k0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k0g RCSB], [http://www.ebi.ac.uk/pdbsum/2k0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2k0g 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=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>
 == Function ==
-[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>
+[[https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2k0g

From Proteopedia

Revision as of 07:30, 27 January 2022

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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