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| | <SX load='6vd7' size='340' side='right' viewer='molstar' caption='[[6vd7]], [[Resolution|resolution]] 3.02Å' scene=''> | | <SX load='6vd7' size='340' side='right' viewer='molstar' caption='[[6vd7]], [[Resolution|resolution]] 3.02Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vd7]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Silurana_(xenopus)_tropicalis Silurana (xenopus) tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VD7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VD7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vd7]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VD7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VD7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">panx1, igdcc4, LOC100170473, nell1, PANX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8364 Silurana (Xenopus) tropicalis])</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]] 3.02Å</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=6vd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vd7 OCA], [http://pdbe.org/6vd7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vd7 RCSB], [http://www.ebi.ac.uk/pdbsum/6vd7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vd7 ProSAT]</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=6vd7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vd7 OCA], [https://pdbe.org/6vd7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vd7 RCSB], [https://www.ebi.ac.uk/pdbsum/6vd7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vd7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B3DLA5_XENTR B3DLA5_XENTR]] Structural component of the gap junctions and the hemichannels.[RuleBase:RU010713] | + | [https://www.uniprot.org/uniprot/B3DLA5_XENTR B3DLA5_XENTR] Structural component of the gap junctions and the hemichannels.[RuleBase:RU010713] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6vd7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6vd7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pannexin|Pannexin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </SX> | | </SX> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Furukawa, H]] | + | [[Category: Xenopus tropicalis]] |
| - | [[Category: Kawate, T]] | + | [[Category: Furukawa H]] |
| - | [[Category: Michalski, M]] | + | [[Category: Kawate T]] |
| - | [[Category: Syrjanen, J L]] | + | [[Category: Michalski M]] |
| - | [[Category: Atp release]]
| + | [[Category: Syrjanen JL]] |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Heptamer]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
B3DLA5_XENTR Structural component of the gap junctions and the hemichannels.[RuleBase:RU010713]
Publication Abstract from PubMed
Pannexins are large-pore forming channels responsible for ATP release under a variety of physiological and pathological conditions. Although predicted to share similar membrane topology with other large-pore forming proteins such as connexins, innexins, and LRRC8, pannexins have minimal sequence similarity to these protein families. Here, we present the cryo-EM structure of a frog pannexin 1 (Panx1) channel at 3.0 A. We find that Panx1 protomers harbor four transmembrane helices similar in arrangement to other large-pore forming proteins but assemble as a heptameric channel with a unique constriction formed by Trp74 in the first extracellular loop. Mutating Trp74 or the nearby Arg75 disrupt ion selectivity whereas altering residues in the hydrophobic groove formed by the two extracellular loops abrogates channel inhibition by carbenoxolone. Our structural and functional study establishes the extracellular loops as important structural motifs for ion selectivity and channel inhibition in Panx1.
The cryo-EM structure of a pannexin 1 reveals unique motifs for ion selection and inhibition.,Michalski K, Syrjanen JL, Henze E, Kumpf J, Furukawa H, Kawate T Elife. 2020 Feb 12;9. pii: 54670. doi: 10.7554/eLife.54670. PMID:32048993[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Michalski K, Syrjanen JL, Henze E, Kumpf J, Furukawa H, Kawate T. The cryo-EM structure of a pannexin 1 reveals unique motifs for ion selection and inhibition. Elife. 2020 Feb 12;9. pii: 54670. doi: 10.7554/eLife.54670. PMID:32048993 doi:http://dx.doi.org/10.7554/eLife.54670
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