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9hex
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 9hex is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==CryoEM structure of mouse Panx1 phosphorylated in vitro by Src== | |
| - | + | <StructureSection load='9hex' size='340' side='right'caption='[[9hex]], [[Resolution|resolution]] 3.56Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9hex]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HEX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HEX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.56Å</td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9hex FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hex OCA], [https://pdbe.org/9hex PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hex RCSB], [https://www.ebi.ac.uk/pdbsum/9hex PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hex ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PANX1_MOUSE PANX1_MOUSE] Ion channel involved in a variety of physiological functions such as blood pressure regulation, apoptotic cell clearance and oogenesis (PubMed:30814251). Forms anion-selective channels with relatively low conductance and an order of permeabilities: nitrate>iodide>chlroride>>aspartate=glutamate=gluconate (PubMed:22311122). Can release ATP upon activation through phosphorylation or cleavage at C-terminus (PubMed:32238926). May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis (By similarity).[UniProtKB:Q96RD7]<ref>PMID:22311122</ref> <ref>PMID:30814251</ref> <ref>PMID:32238926</ref> During apoptosis and after cleavage by caspases of the C-terminal tail, acts as a plasma membrane channel which mediates the regulated release of find-me signals, such as nucleotides ATP and UTP, and selective plasme membrane permeability.<ref>PMID:32238926</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Dahl G]] | ||
| + | [[Category: Gaullier G]] | ||
| + | [[Category: Mim C]] | ||
| + | [[Category: Zhang Q]] | ||
Current revision
CryoEM structure of mouse Panx1 phosphorylated in vitro by Src
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Categories: Large Structures | Mus musculus | Dahl G | Gaullier G | Mim C | Zhang Q
