4alx: Difference between revisions
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==Crystal Structure of Ls-AChBP complexed with the potent nAChR antagonist DHbE== | ==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=''> | <StructureSection load='4alx' size='340' side='right'caption='[[4alx]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4alx]] is a 10 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4alx]] is a 10 chain structure with sequence from [https://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 [https://proteopedia.org/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> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4alx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4alx OCA], [https://pdbe.org/4alx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4alx RCSB], [https://www.ebi.ac.uk/pdbsum/4alx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4alx ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST] Binds to acetylcholine. Modulates neuronal synaptic transmission. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4alx" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Acetylcholine binding protein|Acetylcholine binding protein]] | *[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lymnaea stagnalis]] | [[Category: Lymnaea stagnalis]] | ||
[[Category: Balle | [[Category: Balle T]] | ||
[[Category: Gajhede | [[Category: Gajhede M]] | ||
[[Category: Kastrup | [[Category: Kastrup JS]] | ||
[[Category: Kristensen | [[Category: Kristensen JL]] | ||
[[Category: Nielsen | [[Category: Nielsen EO]] | ||
[[Category: Shahsavar | [[Category: Shahsavar A]] | ||
Latest revision as of 11:17, 23 October 2024
Crystal Structure of Ls-AChBP complexed with the potent nAChR antagonist DHbECrystal Structure of Ls-AChBP complexed with the potent nAChR antagonist DHbE
Structural highlights
FunctionACHP_LYMST Binds to acetylcholine. Modulates neuronal synaptic transmission. Publication Abstract from PubMedNicotinic 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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