1q5o: Difference between revisions

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-[[Image:1q5o.jpg|left|200px]]
- {{Structure
+==HCN2J 443-645 in the presence of cAMP, selenomethionine derivative==
-|PDB= 1q5o |SIZE=350|CAPTION= <scene name='initialview01'>1q5o</scene>, resolution 2.3&Aring;
+<StructureSection load='1q5o' size='340' side='right'caption='[[1q5o]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CMP:ADENOSINE-3&#39;,5&#39;-CYCLIC-MONOPHOSPHATE'>CMP</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE= HCN2, BCNG2 OR HAC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus])
+<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>
-}}
+<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>
+</table>
+== Function ==
+[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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q5/1q5o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''HCN2J 443-645 in the presence of cAMP, selenomethionine derivative'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1q5o" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Ion channels 3D structures|Ion channels 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-Q5O is a [[Single protein]] structure of 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=1Q5O OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-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://www.ncbi.nlm.nih.gov/pubmed/12968185 12968185]
 [[Category: Mus musculus]]
-[[Category: Single protein]]
+[[Category: Black KD]]
-[[Category: Black, K D.]]
+[[Category: Gouaux JE]]
-[[Category: Gouaux, J E.]]
+[[Category: Olivier NB]]
-[[Category: Olivier, N B.]]
+[[Category: Olson R]]
-[[Category: Olson, R.]]
+[[Category: Young EC]]
-[[Category: Young, E C.]]
+[[Category: Zagotta WN]]
-[[Category: Zagotta, W N.]]
-[[Category: CMP]]
-[[Category: c-linker]]
-[[Category: camp]]
-[[Category: cap]]
-[[Category: channel]]
-[[Category: cnbd]]
-[[Category: cyclic nucleotide]]
-[[Category: hcn]]
-[[Category: hcn2]]
-[[Category: ion channel]]
-[[Category: ligand]]
-[[Category: pacemaker]]
-[[Category: pka]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:17:55 2008''