2q0a
From Proteopedia
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(New page: 200px<br /><applet load="2q0a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2q0a, resolution 2.250Å" /> '''Structure and rearr...) |
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| - | [[Image:2q0a.gif|left|200px]]<br /><applet load="2q0a" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2q0a, resolution 2.250Å" /> | ||
| - | '''Structure and rearrangements in the carboxy-terminal region of SpIH channels'''<br /> | ||
| - | == | + | ==Structure and rearrangements in the carboxy-terminal region of SpIH channels== |
| - | + | <StructureSection load='2q0a' size='340' side='right'caption='[[2q0a]], [[Resolution|resolution]] 2.25Å' scene=''> | |
| - | [[ | + | == Structural highlights == |
| - | [[ | + | <table><tr><td colspan='2'>[[2q0a]] 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=2Q0A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Q0A FirstGlance]. <br> |
| - | [[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | [ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</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=2q0a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q0a OCA], [https://pdbe.org/2q0a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2q0a RCSB], [https://www.ebi.ac.uk/pdbsum/2q0a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2q0a 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/q0/2q0a_consurf.spt"</scriptWhenChecked> | |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2q0a ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hyperpolarization-activated cyclic nucleotide-modulated (HCN) ion channels regulate the spontaneous firing activity and electrical excitability of many cardiac and neuronal cells. The modulation of HCN channel opening by the direct binding of cAMP underlies many physiological processes such as the autonomic regulation of the heart rate. Here we use a combination of X-ray crystallography and electrophysiology to study the allosteric mechanism for cAMP modulation of HCN channels. SpIH is an invertebrate HCN channel that is activated fully by cAMP, but only partially by cGMP. We exploited the partial agonist action of cGMP on SpIH to reveal the molecular mechanism for cGMP specificity of many cyclic nucleotide-regulated enzymes. Our results also elaborate a mechanism for the allosteric conformational change in the cyclic nucleotide-binding domain and a mechanism for partial agonist action. These mechanisms will likely extend to other cyclic nucleotide-regulated channels and enzymes as well. | ||
| - | + | Structure and rearrangements in the carboxy-terminal region of SpIH channels.,Flynn GE, Black KD, Islas LD, Sankaran B, Zagotta WN Structure. 2007 Jun;15(6):671-82. PMID:17562314<ref>PMID:17562314</ref> | |
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2q0a" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Black KD]] | ||
| + | [[Category: Flynn GE]] | ||
| + | [[Category: Islas LD]] | ||
| + | [[Category: Sankaran B]] | ||
| + | [[Category: Zagotta WN]] | ||
Current revision
Structure and rearrangements in the carboxy-terminal region of SpIH channels
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