1q5o

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(New page: 200px<br /><applet load="1q5o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q5o, resolution 2.3&Aring;" /> '''HCN2J 443-645 in the ...)
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[[Image:1q5o.jpg|left|200px]]<br /><applet load="1q5o" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1q5o, resolution 2.3&Aring;" />
 
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'''HCN2J 443-645 in the presence of cAMP, selenomethionine derivative'''<br />
 
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==Overview==
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==HCN2J 443-645 in the presence of cAMP, selenomethionine derivative==
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The family of hyperpolarization-activated, cyclic nucleotide-modulated, (HCN) channels are crucial for a range of electrical signalling, including, cardiac and neuronal pacemaker activity, setting resting membrane, electrical properties and dendritic integration. These nonselective cation, channels, underlying the I(f), I(h) and I(q) currents of heart and nerve, cells, are activated by membrane hyperpolarization and modulated by the, binding of cyclic nucleotides such as cAMP and cGMP. The cAMP-mediated, enhancement of channel activity is largely responsible for the increase in, heart rate caused by beta-adrenergic agonists. Here we have investigated, the mechanism underlying this modulation by studying a carboxy-terminal, fragment of HCN2 containing the cyclic nucleotide-binding domain (CNBD), and the C-linker region that connects the CNBD to the pore. X-ray, crystallographic structures of this C-terminal fragment bound to cAMP or, cGMP, together with equilibrium sedimentation analysis, identify a, tetramerization domain and the mechanism for cyclic nucleotide, specificity, and suggest a model for ligand-dependent channel modulation., On the basis of amino acid sequence similarity to HCN channels, the cyclic, nucleotide-gated, and eag- and KAT1-related families of channels are, probably related to HCN channels in structure and mechanism.
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<StructureSection load='1q5o' size='340' side='right'caption='[[1q5o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1q5o]] is a 1 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=1Q5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q5O FirstGlance]. <br>
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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]] 2.3&#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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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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=1q5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5o OCA], [https://pdbe.org/1q5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q5o RCSB], [https://www.ebi.ac.uk/pdbsum/1q5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q5o 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/q5/1q5o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1q5o 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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The family of hyperpolarization-activated, cyclic nucleotide-modulated (HCN) channels are crucial for a range of electrical signalling, including cardiac and neuronal pacemaker activity, setting resting membrane electrical properties and dendritic integration. These nonselective cation channels, underlying the I(f), I(h) and I(q) currents of heart and nerve cells, are activated by membrane hyperpolarization and modulated by the binding of cyclic nucleotides such as cAMP and cGMP. The cAMP-mediated enhancement of channel activity is largely responsible for the increase in heart rate caused by beta-adrenergic agonists. Here we have investigated the mechanism underlying this modulation by studying a carboxy-terminal fragment of HCN2 containing the cyclic nucleotide-binding domain (CNBD) and the C-linker region that connects the CNBD to the pore. X-ray crystallographic structures of this C-terminal fragment bound to cAMP or cGMP, together with equilibrium sedimentation analysis, identify a tetramerization domain and the mechanism for cyclic nucleotide specificity, and suggest a model for ligand-dependent channel modulation. On the basis of amino acid sequence similarity to HCN channels, the cyclic nucleotide-gated, and eag- and KAT1-related families of channels are probably related to HCN channels in structure and mechanism.
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==About this Structure==
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Structural basis for modulation and agonist specificity of HCN pacemaker channels.,Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, Gouaux E Nature. 2003 Sep 11;425(6954):200-5. PMID:12968185<ref>PMID:12968185</ref>
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1Q5O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with CMP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q5O OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for modulation and agonist specificity of HCN pacemaker channels., Zagotta WN, Olivier NB, Black KD, Young EC, Olson R, Gouaux E, Nature. 2003 Sep 11;425(6954):200-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12968185 12968185]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1q5o" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Black, K.D.]]
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[[Category: Gouaux, J.E.]]
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[[Category: Olivier, N.B.]]
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[[Category: Olson, R.]]
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[[Category: Young, E.C.]]
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[[Category: Zagotta, W.N.]]
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[[Category: CMP]]
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[[Category: c-linker]]
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[[Category: camp]]
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[[Category: cap]]
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[[Category: channel]]
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[[Category: cnbd]]
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[[Category: cyclic nucleotide]]
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[[Category: hcn]]
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[[Category: hcn2]]
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[[Category: ion channel]]
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[[Category: ligand]]
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[[Category: pacemaker]]
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[[Category: pka]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:24:15 2007''
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Black KD]]
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[[Category: Gouaux JE]]
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[[Category: Olivier NB]]
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[[Category: Olson R]]
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[[Category: Young EC]]
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[[Category: Zagotta WN]]

Current revision

HCN2J 443-645 in the presence of cAMP, selenomethionine derivative

PDB ID 1q5o

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