3beh: Difference between revisions
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<StructureSection load='3beh' size='340' side='right' caption='[[3beh]], [[Resolution|resolution]] 3.10Å' scene=''> | <StructureSection load='3beh' size='340' side='right' caption='[[3beh]], [[Resolution|resolution]] 3.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3beh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3beh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33669 Atcc 33669]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BEH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BEH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3beh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3beh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3beh RCSB], [http://www.ebi.ac.uk/pdbsum/3beh PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3beh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3beh OCA], [http://pdbe.org/3beh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3beh RCSB], [http://www.ebi.ac.uk/pdbsum/3beh PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=3beh ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3beh" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Atcc 33669]] | ||
[[Category: Clayton, G M]] | [[Category: Clayton, G M]] | ||
[[Category: Morais-Cabral, J H]] | [[Category: Morais-Cabral, J H]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Transmembrane protein]] | [[Category: Transmembrane protein]] | ||
Revision as of 18:33, 9 February 2016
Structure of a Bacterial Cyclic Nucleotide Regulated Ion ChannelStructure of a Bacterial Cyclic Nucleotide Regulated Ion Channel
Structural highlights
Function[CNGK1_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 PubMedThe six-transmembrane helix (6 TM) tetrameric cation channels form the largest ion channel family, some members of which are voltage-gated and others are not. There are no reported channel structures to match the wealth of functional data on the non-voltage-gated members. We determined the structure of the transmembrane regions of the bacterial cyclic nucleotide-regulated channel MlotiK1, a non-voltage-gated 6 TM channel. The structure showed how the S1-S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing. Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel.,Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1511-5. Epub 2008 Jan 23. PMID:18216238[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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