6v3g
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of Ca2+-free hsSlo1 channel== | |
| + | <StructureSection load='6v3g' size='340' side='right'caption='[[6v3g]], [[Resolution|resolution]] 4.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6v3g]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V3G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6V3G FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6v22|6v22]]</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=6v3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v3g OCA], [http://pdbe.org/6v3g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v3g RCSB], [http://www.ebi.ac.uk/pdbsum/6v3g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v3g ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Slo1 is a Ca(2+)- and voltage-activated K(+) channel that underlies skeletal and smooth muscle contraction, audition, hormone secretion and neurotransmitter release. In mammals, Slo1 is regulated by auxiliary proteins that confer tissue-specific gating and pharmacological properties. This study presents cryo-EM structures of Slo1 in complex with the auxiliary protein, beta4. Four beta4, each containing two transmembrane helices, encircle Slo1, contacting it through helical interactions inside the membrane. On the extracellular side, b4 forms a tetrameric crown over the pore. Structures with high and low Ca(2+) concentrations show that identical gating conformations occur in the absence and presence of beta4, implying that beta4 serves to modulate the relative stabilities of 'pre-existing' conformations rather than creating new ones. The effects of beta4 on scorpion toxin inhibition kinetics are explained by the crown, which constrains access but does not prevent binding. | ||
| - | + | Molecular structures of the human Slo1 K(+) channel in complex with beta4.,Tao X, MacKinnon R Elife. 2019 Dec 9;8. pii: 51409. doi: 10.7554/eLife.51409. PMID:31815672<ref>PMID:31815672</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6v3g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: MacKinnon, R]] | ||
| + | [[Category: Tao, X]] | ||
| + | [[Category: Bk channel]] | ||
| + | [[Category: High conductance ca2+-activated k+ channel]] | ||
| + | [[Category: Maxik channel]] | ||
| + | [[Category: Slo1 channel]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 09:23, 25 December 2019
Cryo-EM structure of Ca2+-free hsSlo1 channel
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