3or6: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3or6.png|left|200px]]
+==On the structural basis of modal gating behavior in K+channels - E71Q==
+<StructureSection load='3or6' size='340' side='right' caption='[[3or6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3or6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OR6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OR6 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></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3or7|3or7]]</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=3or6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3or6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3or6 RCSB], [http://www.ebi.ac.uk/pdbsum/3or6 PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Modal-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.
-{{STRUCTURE_3or6|  PDB=3or6  |  SCENE=  }}
+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<ref>PMID:21186363</ref>
-===On the structural basis of modal gating behavior in K+channels - E71Q===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_21186363}}
-==About this Structure==
-[[3or6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OR6 OCA].
 ==See Also==
 *[[Antibody|Antibody]]
 *[[Potassium Channel|Potassium Channel]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:021186363</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Mus musculus]]
 [[Category: Streptomyces lividans]]
-[[Category: Chakrapani, S.]]
+[[Category: Chakrapani, S]]
-[[Category: Cordero-Morales, J F.]]
+[[Category: Cordero-Morales, J F]]
-[[Category: Jogini, V.]]
+[[Category: Jogini, V]]
-[[Category: Perozo, E.]]
+[[Category: Perozo, E]]
 [[Category: Alpha-helical]]
 [[Category: Immune system-transport protein complex]]
 [[Category: Inactivation]]
 [[Category: Potassium channel]]