6by3: Difference between revisions

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<StructureSection load='6by3' size='340' side='right' caption='[[6by3]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
<StructureSection load='6by3' size='340' side='right' caption='[[6by3]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6by3]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BY3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6by3]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Strco Strco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BY3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BY3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <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=DGA:DIACYL+GLYCEROL'>DGA</scene>, <scene name='pdbligand=F09:NONAN-1-OL'>F09</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kcsA, skc1, SCO7660, SC10F4.33 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=100226 STRCO])</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=6by3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6by3 OCA], [http://pdbe.org/6by3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6by3 RCSB], [http://www.ebi.ac.uk/pdbsum/6by3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6by3 ProSAT]</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=6by3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6by3 OCA], [http://pdbe.org/6by3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6by3 RCSB], [http://www.ebi.ac.uk/pdbsum/6by3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6by3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/KCSA_STRCO KCSA_STRCO]] Acts as a potassium ion channel (By similarity).  
[[http://www.uniprot.org/uniprot/KCSA_STRCO KCSA_STRCO]] Acts as a potassium ion channel (By similarity).  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The selectivity filter and the activation gate in potassium channels are functionally and structurally coupled. An allosteric coupling underlies C-type inactivation coupled to activation gating in this ion-channel family (i.e., opening of the activation gate triggers the collapse of the channel's selectivity filter). We have identified the second Threonine residue within the TTVGYGD signature sequence of K(+) channels as a crucial residue for this allosteric communication. A Threonine to Alanine substitution at this position was studied in three representative members of the K(+)-channel family. Interestingly, all of the mutant channels exhibited lack of C-type inactivation gating and an inversion of their allosteric coupling (i.e., closing of the activation gate collapses the channel's selectivity filter). A state-dependent crystallographic study of KcsA-T75A proves that, on activation, the selectivity filter transitions from a nonconductive and deep C-type inactivated conformation to a conductive one. Finally, we provide a crystallographic demonstration that closed-state inactivation can be achieved by the structural collapse of the channel's selectivity filter.
Inverted allosteric coupling between activation and inactivation gates in K(+) channels.,Labro AJ, Cortes DM, Tilegenova C, Cuello LG Proc Natl Acad Sci U S A. 2018 May 7. pii: 1800559115. doi:, 10.1073/pnas.1800559115. PMID:29735651<ref>PMID:29735651</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6by3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Strco]]
[[Category: Cortes, D M]]
[[Category: Cortes, D M]]
[[Category: Cuello, L G]]
[[Category: Cuello, L G]]

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