View source for 4alx


==Crystal Structure of Ls-AChBP complexed with the potent nAChR antagonist DHbE==
<StructureSection load='4alx' size='340' side='right' caption='[[4alx]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4alx]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Great_pond_snail Great pond snail]. 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 id='ligand'><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></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1i9b|1i9b]], [[1uv6|1uv6]], [[1uw6|1uw6]], [[1ux2|1ux2]]</td></tr>
<tr id='resources'><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://pdbe.org/4alx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4alx RCSB], [http://www.ebi.ac.uk/pdbsum/4alx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4alx ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST]] Binds to acetylcholine. Modulates neuronal synaptic transmission. 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4alx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acetylcholine binding protein|Acetylcholine binding protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Great pond snail]]
[[Category: Balle, T]]
[[Category: Gajhede, M]]
[[Category: Kastrup, J S]]
[[Category: Kristensen, J L]]
[[Category: Nielsen, E O]]
[[Category: Shahsavar, A]]
[[Category: Acetylcholine-binding protein]]
[[Category: Antagonist]]
[[Category: C-loop]]
[[Category: Dihydro-b-erythroidine]]
[[Category: Lymnaea stagnali]]