3or7: Difference between revisions
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==On the structural basis of modal gating behavior in K+channels - E71I== | ==On the structural basis of modal gating behavior in K+channels - E71I== | ||
<StructureSection load='3or7' size='340' side='right' caption='[[3or7]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3or7' size='340' side='right' caption='[[3or7]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3or6|3or6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3or6|3or6]]</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=3or7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3or7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3or7 RCSB], [http://www.ebi.ac.uk/pdbsum/3or7 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=3or7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3or7 OCA], [http://pdbe.org/3or7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3or7 RCSB], [http://www.ebi.ac.uk/pdbsum/3or7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3or7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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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 3or7" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Potassium Channel|Potassium Channel]] | *[[Potassium Channel|Potassium Channel]] | ||
*[[3D structures of antibody|3D structures of antibody]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 05:49, 5 August 2016
On the structural basis of modal gating behavior in K+channels - E71IOn the structural basis of modal gating behavior in K+channels - E71I
Structural highlights
Function[KCSA_STRLI] Acts as a pH-gated potassium ion channel; changing the cytosolic pH from 7 to 4 opens the channel, although it is not clear if this is the physiological stimulus for channel opening. Monovalent cation preference is K(+) > Rb(+) > NH4(+) >> Na(+) > Li(+).[1] Publication Abstract from PubMedModal-gating shifts represent an effective regulatory mechanism by which ion channels control the extent and time course of ionic fluxes. Under steady-state conditions, the K(+) channel KcsA shows three distinct gating modes, high-P(o), low-P(o) and a high-frequency flicker mode, each with about an order of magnitude difference in their mean open times. Here we show that in the absence of C-type inactivation, mutations at the pore-helix position Glu71 unmask a series of kinetically distinct modes of gating in a side chain-specific way. These gating modes mirror those seen in wild-type channels and suggest that specific interactions in the side chain network surrounding the selectivity filter, in concert with ion occupancy, alter the relative stability of pre-existing conformational states of the pore. The present results highlight the key role of the selectivity filter in regulating modal gating behavior in K(+) channels. On the structural basis of modal gating behavior in K(+) channels.,Chakrapani S, Cordero-Morales JF, Jogini V, Pan AC, Cortes DM, Roux B, Perozo E Nat Struct Mol Biol. 2011 Jan;18(1):67-74. Epub 2010 Dec 26. PMID:21186363[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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