1vp6: Difference between revisions
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New page: left|200px<br /><applet load="1vp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vp6, resolution 1.70Å" /> '''M.loti ion channel c... |
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== | ==M.loti ion channel cylic nucleotide binding domain== | ||
Here we describe the initial functional characterization of a cyclic | <StructureSection load='1vp6' size='340' side='right'caption='[[1vp6]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1vp6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pf0 1pf0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VP6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VP6 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]] 1.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</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=1vp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vp6 OCA], [https://pdbe.org/1vp6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vp6 RCSB], [https://www.ebi.ac.uk/pdbsum/1vp6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vp6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</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/vp/1vp6_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=1vp6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Here we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices. | |||
Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel.,Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH Cell. 2004 Nov 24;119(5):615-27. PMID:15550244<ref>PMID:15550244</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1vp6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
*[[Potassium channel 3D structures|Potassium channel 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mesorhizobium loti]] | [[Category: Mesorhizobium loti]] | ||
[[Category: Clayton GM]] | |||
[[Category: Clayton | [[Category: Heginbotham L]] | ||
[[Category: Heginbotham | [[Category: Morais-Cabral JH]] | ||
[[Category: Morais-Cabral | [[Category: Silverman WR]] | ||
[[Category: Silverman | |||
Latest revision as of 03:05, 28 December 2023
M.loti ion channel cylic nucleotide binding domainM.loti ion channel cylic nucleotide binding domain
Structural highlights
FunctionCNGK1_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 PubMedHere we describe the initial functional characterization of a cyclic nucleotide regulated ion channel from the bacterium Mesorhizobium loti and present two structures of its cyclic nucleotide binding domain, with and without cAMP. The domains are organized as dimers with the interface formed by the linker regions that connect the nucleotide binding pocket to the pore domain. Together, structural and functional data suggest the domains form two dimers on the cytoplasmic face of the channel. We propose a model for gating in which ligand binding alters the structural relationship within a dimer, directly affecting the position of the adjacent transmembrane helices. Structural basis of ligand activation in a cyclic nucleotide regulated potassium channel.,Clayton GM, Silverman WR, Heginbotham L, Morais-Cabral JH Cell. 2004 Nov 24;119(5):615-27. PMID:15550244[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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