3or7

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Revision as of 11:18, 21 February 2024

On the structural basis of modal gating behavior in K+channels - E71I

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Retrieved from "http://52.214.119.220/wiki/index.php/3or7"

@@ Line 3: / Line 3: @@
 <StructureSection load='3or7' size='340' side='right'caption='[[3or7]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3or7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_lividans"_krasil'nikov_et_al._1965 "actinomyces lividans" krasil'nikov et al. 1965] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OR7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3or7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OR7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3or6|3or6]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</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=3or7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3or7 OCA], [https://pdbe.org/3or7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3or7 RCSB], [https://www.ebi.ac.uk/pdbsum/3or7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3or7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KCSA_STRLI 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(+).<ref>PMID:7489706</ref>
+[https://www.uniprot.org/uniprot/KCSA_STRLI 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(+).<ref>PMID:7489706</ref>
-<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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3or7" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 28: / Line 19: @@
 __TOC__
 </StructureSection>
-[[Category: Actinomyces lividans krasil'nikov et al. 1965]]
 [[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Chakrapani, S]]
+[[Category: Streptomyces lividans]]
-[[Category: Cordero-Morales, J F]]
+[[Category: Chakrapani S]]
-[[Category: Cortes, D M]]
+[[Category: Cordero-Morales JF]]
-[[Category: Jogini, V]]
+[[Category: Cortes DM]]
-[[Category: Pan, A C]]
+[[Category: Jogini V]]
-[[Category: Perozo, E]]
+[[Category: Pan AC]]
-[[Category: Roux, B]]
+[[Category: Perozo E]]
-[[Category: Alpha-helical]]
+[[Category: Roux B]]
-[[Category: Immune system-transport protein complex]]
-[[Category: Inactivation]]
-[[Category: Potassium channel]]

3or7

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Revision as of 11:18, 21 February 2024

On the structural basis of modal gating behavior in K+channels - E71I

Structural highlights

Function

See Also

References

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