3ffq

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[[Image:3ffq.png|left|200px]]
 
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==HCN2I 443-640 apo-state==
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The line below this paragraph, containing "STRUCTURE_3ffq", creates the "Structure Box" on the page.
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<StructureSection load='3ffq' size='340' side='right'caption='[[3ffq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3ffq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FFQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr>
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{{STRUCTURE_3ffq| PDB=3ffq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ffq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffq OCA], [https://pdbe.org/3ffq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ffq RCSB], [https://www.ebi.ac.uk/pdbsum/3ffq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ffq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HCN2_MOUSE HCN2_MOUSE] Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). Can also transport ammonium in the distal nephron. Produces a large instantaneous current. Activated by cAMP. Modulated by intracellular chloride ions and pH; acidic pH shifts the activation to more negative voltages.<ref>PMID:11741901</ref>
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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/ff/3ffq_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/main_output.php?pdb_ID=3ffq 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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Visualizing conformational dynamics in proteins has been difficult, and the atomic-scale motions responsible for the behavior of most allosteric proteins are unknown. Here we report that fluorescence resonance energy transfer (FRET) between a small fluorescent dye and a nickel ion bound to a dihistidine motif can be used to monitor small structural rearrangements in proteins. This method provides several key advantages over classical FRET, including the ability to measure the dynamics of close-range interactions, the use of small probes with short linkers, a low orientation dependence, and the ability to add and remove unique tunable acceptors. We used this 'transition metal ion FRET' approach along with X-ray crystallography to determine the structural changes of the gating ring of the mouse hyperpolarization-activated cyclic nucleotide-regulated ion channel HCN2. Our results suggest a general model for the conformational switch in the cyclic nucleotide-binding site of cyclic nucleotide-regulated ion channels.
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===HCN2I 443-640 apo-state===
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Mapping the structure and conformational movements of proteins with transition metal ion FRET.,Taraska JW, Puljung MC, Olivier NB, Flynn GE, Zagotta WN Nat Methods. 2009 Jul;6(7):532-7. Epub 2009 Jun 14. PMID:19525958<ref>PMID:19525958</ref>
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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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The line below this paragraph, {{ABSTRACT_PUBMED_19525958}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3ffq" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19525958 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19525958}}
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==About this Structure==
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[[3ffq]] is a 2 chain structure of [[Ion channels (Part II)]] with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFQ OCA].
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==See Also==
==See Also==
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*[[Ion channels (Part II)]]
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:19525958</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Olivier, N B.]]
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[[Category: Olivier NB]]
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[[Category: 3d-structure]]
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[[Category: Camp]]
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[[Category: Camp-binding]]
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[[Category: Glycoprotein]]
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[[Category: Ion channel]]
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[[Category: Ion transport]]
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[[Category: Ionic channel]]
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[[Category: Membrane]]
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[[Category: Metal transport]]
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[[Category: Nucleotide-binding]]
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[[Category: Phosphoprotein]]
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[[Category: Potassium]]
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[[Category: Potassium channel]]
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[[Category: Potassium transport]]
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[[Category: Sodium]]
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[[Category: Sodium channel]]
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[[Category: Sodium transport]]
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[[Category: Transmembrane]]
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[[Category: Transport]]
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[[Category: Voltage-gated channel]]
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Current revision

HCN2I 443-640 apo-state

PDB ID 3ffq

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