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==On the structural basis of modal gating behavior in K+channels - E71Q==
==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=''>
<StructureSection load='3or6' size='340' side='right'caption='[[3or6]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== 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>
<table><tr><td colspan='2'>[[3or6]] 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=3OR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3or7|3or7]]</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'>[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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3or6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3or6 OCA], [https://pdbe.org/3or6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3or6 RCSB], [https://www.ebi.ac.uk/pdbsum/3or6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3or6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3or6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Antibody|Antibody]]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Potassium Channel|Potassium Channel]]
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Streptomyces lividans]]
[[Category: Streptomyces lividans]]
[[Category: Chakrapani, S]]
[[Category: Chakrapani S]]
[[Category: Cordero-Morales, J F]]
[[Category: Cordero-Morales JF]]
[[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]]

Latest revision as of 09:36, 27 November 2024

On the structural basis of modal gating behavior in K+channels - E71QOn the structural basis of modal gating behavior in K+channels - E71Q

Structural highlights

3or6 is a 3 chain structure with sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Schrempf H, Schmidt O, Kummerlen R, Hinnah S, Muller D, Betzler M, Steinkamp T, Wagner R. A prokaryotic potassium ion channel with two predicted transmembrane segments from Streptomyces lividans. EMBO J. 1995 Nov 1;14(21):5170-8. PMID:7489706
  2. Chakrapani S, Cordero-Morales JF, Jogini V, Pan AC, Cortes DM, Roux B, Perozo E. On the structural basis of modal gating behavior in K(+) channels. Nat Struct Mol Biol. 2011 Jan;18(1):67-74. Epub 2010 Dec 26. PMID:21186363 doi:10.1038/nsmb.1968

3or6, resolution 2.70Å

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