6v38

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:35, 6 March 2024) (edit) (undo)
 
Line 3: Line 3:
<SX load='6v38' size='340' side='right' viewer='molstar' caption='[[6v38]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<SX load='6v38' size='340' side='right' viewer='molstar' caption='[[6v38]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6v38]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V38 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6V38 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6v38]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6V38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6V38 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6v22|6v22]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KCNMA1, KCNMA, SLO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6v38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v38 OCA], [https://pdbe.org/6v38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6v38 RCSB], [https://www.ebi.ac.uk/pdbsum/6v38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6v38 ProSAT]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6v38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6v38 OCA], [http://pdbe.org/6v38 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6v38 RCSB], [http://www.ebi.ac.uk/pdbsum/6v38 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6v38 ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/KCMA1_HUMAN KCMA1_HUMAN]
-
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>
+
==See Also==
-
 
+
*[[Potassium channel 3D structures|Potassium channel 3D structures]]
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6v38" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</SX>
</SX>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: MacKinnon, R]]
+
[[Category: MacKinnon R]]
-
[[Category: Tao, X]]
+
[[Category: Tao X]]
-
[[Category: Bk channel]]
+
-
[[Category: High conductance ca2+-activated k+ channel]]
+
-
[[Category: Maxik channel]]
+
-
[[Category: Slo1 channel]]
+
-
[[Category: Transport protein]]
+

Current revision

Cryo-EM structure of Ca2+-bound hsSlo1 channel

6v38, resolution 3.80Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6v38"
Personal tools