7txf
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7txf is ON HOLD Authors: Ho, T.N.T., Abraham, N., Lewis, R.J. Description: The allosteric binding mode of alphaD-conotoxin VxXXB [[Category: Unrele...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The allosteric binding mode of alphaD-conotoxin VxXXB== |
| + | <StructureSection load='7txf' size='340' side='right'caption='[[7txf]], [[Resolution|resolution]] 2.47Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7txf]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_vexillum Conus vexillum] and [https://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TXF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TXF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.47Å</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=7txf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7txf OCA], [https://pdbe.org/7txf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7txf RCSB], [https://www.ebi.ac.uk/pdbsum/7txf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7txf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | alphaD-conotoxins are 11 kDa homodimers that potently inhibit nicotinic acetylcholine receptors (nAChRs) through a non-competitive (allosteric) mechanism. In this study, we describe the allosteric binding mode of the granulin-like C-terminal (CTD) of VxXXB bound to Lymnea stagnalis acetylcholine binding protein (Ls-AChBP), a soluble homologue of the extracellular ligand-binding domain of nAChRs. This co-crystal complex revealed a novel allosteric binding site for nAChR antagonists outside the C-loop that caps the orthosteric site defined by the nAChR agonist nicotine and the antagonist epibatidine. Mutational and docking studies on Ls-AChBP supported a two-site binding mode for full-length VxXXB, with the first CTD binding site located outside the C-loop as seen in the co-crystal complex, with a second CTD binding site located near the N-terminal end of the adjacent subunit of AChBP. These results provide new structural insight into a novel allosteric mechanism of nAChR inhibition and define the cooperative binding mode of the N-terminal domain linked granulin core domains of alphaD-conotoxins. | ||
| - | + | Unravelling the allosteric binding mode of alphaD-VxXXB at nicotinic acetylcholine receptors.,Ho TN, Abraham N, Lewis RJ Front Pharmacol. 2023 Apr 13;14:1170514. doi: 10.3389/fphar.2023.1170514. , eCollection 2023. PMID:37124228<ref>PMID:37124228</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7txf" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Abraham | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Conus vexillum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lymnaea stagnalis]] | ||
| + | [[Category: Abraham N]] | ||
| + | [[Category: Ho TNT]] | ||
| + | [[Category: Lewis RJ]] | ||
Current revision
The allosteric binding mode of alphaD-conotoxin VxXXB
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