6n24
From Proteopedia
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(New page: '''Unreleased structure''' The entry 6n24 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==BEST1 open state W287F mutant, calcium-free== | |
| + | <SX load='6n24' size='340' side='right' viewer='molstar' caption='[[6n24]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6n24]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N24 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]] 3Å</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=6n24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n24 OCA], [https://pdbe.org/6n24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n24 RCSB], [https://www.ebi.ac.uk/pdbsum/6n24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n24 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bestrophin (BEST1-4) ligand-gated chloride (Cl(-)) channels are activated by calcium (Ca(2+)). Mutation of BEST1 causes retinal disease. Partly because bestrophin channels have no sequence or structural similarity to other ion channels, the molecular mechanisms underlying gating are unknown. Here, we present a series of cryo-electron microscopy structures of chicken BEST1, determined at 3.1 A resolution or better, that represent the channel's principal gating states. Unlike other channels, opening of the pore is due to the repositioning of tethered pore-lining helices within a surrounding protein shell that dramatically widens a neck of the pore through a concertina of amino acid rearrangements. The neck serves as both the activation and the inactivation gate. Ca(2+) binding instigates opening of the neck through allosteric means whereas inactivation peptide binding induces closing. An aperture within the otherwise wide pore controls anion permeability. The studies define a new molecular paradigm for gating among ligand-gated ion channels. | ||
| - | + | Molecular mechanisms of gating in the calcium-activated chloride channel bestrophin.,Miller AN, Vaisey G, Long SB Elife. 2019 Jan 10;8. pii: 43231. doi: 10.7554/eLife.43231. PMID:30628889<ref>PMID:30628889</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6n24" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Bestrophin 3D structures|Bestrophin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </SX> | ||
| + | [[Category: Gallus gallus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Long SB]] | ||
| + | [[Category: Miller AN]] | ||
| + | [[Category: Vaisey G]] | ||
Current revision
BEST1 open state W287F mutant, calcium-free
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