4alx: Difference between revisions
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[[ | ==Crystal Structure of Ls-AChBP complexed with the potent nAChR antagonist DHbE== | ||
<StructureSection load='4alx' size='340' side='right' caption='[[4alx]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4alx]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ALX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ALX FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=IZN:(4BS,6S)-6-METHOXY-1,4,6,7,9,10,12,13-OCTAHYDRO-3H,5H-PYRANO[4,3 3,4]PYRIDO[2,1-I]INDOL-3-ONE'>IZN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i9b|1i9b]], [[1uv6|1uv6]], [[1uw6|1uw6]], [[1ux2|1ux2]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4alx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4alx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4alx RCSB], [http://www.ebi.ac.uk/pdbsum/4alx PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nicotinic acetylcholine receptors (nAChRs) are pentameric ligand-gated ion channels that belong to the Cys-loop receptor superfamily. These receptors are allosteric proteins that exist in different conformational states, including resting (closed), activated (open), and desensitized (closed) states. The acetylcholine binding protein (AChBP) is a structural homologue of the extracellular ligand-binding domain of nAChRs. In previous studies, the degree of the C-loop radial extension of AChBP has been assigned to different conformational states of nAChRs. It has been suggested that a closed C-loop is preferred for the active conformation of nAChRs in complex with agonists whereas an open C-loop reflects an antagonist-bound (closed) state. In this work, we have determined the crystal structure of AChBP from the water snail Lymnaea stagnalis (Ls) in complex with dihydro-beta-erythroidine (DHbetaE), which is a potent competitive antagonist of nAChRs. The structure reveals that binding of DHbetaE to AChBP imposes closure of the C-loop as agonists, but also a shift perpendicular to previously observed C-loop movements. These observations suggest that DHbetaE may antagonize the receptor via a different mechanism compared to prototypical antagonists and toxins. | |||
Crystal Structure of Lymnaea stagnalis AChBP Complexed with the Potent nAChR Antagonist DHbetaE Suggests a Unique Mode of Antagonism.,Shahsavar A, Kastrup JS, Nielsen EO, Kristensen JL, Gajhede M, Balle T PLoS One. 2012;7(8):e40757. Epub 2012 Aug 22. PMID:22927902<ref>PMID:22927902</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Acetylcholine binding protein|Acetylcholine binding protein]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lymnaea stagnalis]] | [[Category: Lymnaea stagnalis]] | ||
[[Category: Balle, T.]] | [[Category: Balle, T.]] | ||
