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| | <StructureSection load='3clp' size='340' side='right'caption='[[3clp]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3clp' size='340' side='right'caption='[[3clp]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3clp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhizobium_loti Rhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CLP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3clp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_loti Rhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CLP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vp6|1vp6]], [[1u12|1u12]], [[3beh|3beh]], [[3cl1|3cl1]], [[3co2|3co2]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1vp6|1vp6]], [[1u12|1u12]], [[3beh|3beh]], [[3cl1|3cl1]], [[3co2|3co2]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3clp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3clp OCA], [http://pdbe.org/3clp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3clp RCSB], [http://www.ebi.ac.uk/pdbsum/3clp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3clp 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=3clp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3clp OCA], [https://pdbe.org/3clp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3clp RCSB], [https://www.ebi.ac.uk/pdbsum/3clp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3clp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| 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 PubMed
MlotiK1 is a prokaryotic homolog of cyclic-nucleotide-dependent ion channels that contains an intracellular C-terminal cyclic nucleotide binding (CNB) domain. X-ray structures of the CNB domain have been solved in the absence of ligand and bound to cAMP. Both the full-length channel and CNB domain fragment are easily expressed and purified, making MlotiK1 a useful model system for dissecting activation by ligand binding. We have used X-ray crystallography to determine three new MlotiK1 CNB domain structures: a second apo configuration, a cGMP-bound structure, and a second cAMP-bound structure. In combination, the five MlotiK1 CNB domain structures provide a unique opportunity for analyzing, within a single protein, the structural differences between the apo state and the bound state, and the structural variability within each state. With this analysis as a guide, we have probed the nucleotide selectivity and importance of specific residue side chains in ligand binding and channel activation. These data help to identify ligand-protein interactions that are important for ligand dependence in MlotiK1 and, more globally, in the class of nucleotide-dependent proteins.
Structural and energetic analysis of activation by a cyclic nucleotide binding domain.,Altieri SL, Clayton GM, Silverman WR, Olivares AO, De la Cruz EM, Thomas LR, Morais-Cabral JH J Mol Biol. 2008 Sep 5;381(3):655-69. Epub 2008 Jun 10. PMID:18619611[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Altieri SL, Clayton GM, Silverman WR, Olivares AO, De la Cruz EM, Thomas LR, Morais-Cabral JH. Structural and energetic analysis of activation by a cyclic nucleotide binding domain. J Mol Biol. 2008 Sep 5;381(3):655-69. Epub 2008 Jun 10. PMID:18619611 doi:10.1016/j.jmb.2008.06.011
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