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[[Image:2bys.gif|left|200px]]<br /><applet load="2bys" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2bys, resolution 2.05&Aring;" />
'''CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA IN COMPLEX WITH LOBELINE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ACHBP FROM APLYSIA CALIFORNICA IN complex with lobeline==
Upon ligand binding at the subunit interfaces, the extracellular domain of, the nicotinic acetylcholine receptor undergoes conformational changes, and, agonist binding allosterically triggers opening of the ion channel. The, soluble acetylcholine-binding protein (AChBP) from snail has been shown to, be a structural and functional surrogate of the ligand-binding domain, (LBD) of the receptor. Yet, individual AChBP species display disparate, affinities for nicotinic ligands. The crystal structure of AChBP from, Aplysia californica in the apo form reveals a more open loop C and, distinctive positions for other surface loops, compared with previous, structures. Analysis of Aplysia AChBP complexes with nicotinic ligands, shows that loop C, which does not significantly change conformation upon, binding of the antagonist, methyllycaconitine, further opens to, accommodate the peptidic antagonist, alpha-conotoxin ImI, but wraps around, the agonists lobeline and epibatidine. The structures also reveal extended, and nonoverlapping interaction surfaces for the two antagonists, outside, the binding loci for agonists. This comprehensive set of structures, reflects a dynamic template for delineating further conformational changes, of the LBD of the nicotinic receptor.
<StructureSection load='2bys' size='340' side='right'caption='[[2bys]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bys]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BYS 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LOB:LOBELINE'>LOB</scene></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=2bys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bys OCA], [https://pdbe.org/2bys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bys RCSB], [https://www.ebi.ac.uk/pdbsum/2bys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bys ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8WSF8_APLCA Q8WSF8_APLCA]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/2bys_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bys ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Upon ligand binding at the subunit interfaces, the extracellular domain of the nicotinic acetylcholine receptor undergoes conformational changes, and agonist binding allosterically triggers opening of the ion channel. The soluble acetylcholine-binding protein (AChBP) from snail has been shown to be a structural and functional surrogate of the ligand-binding domain (LBD) of the receptor. Yet, individual AChBP species display disparate affinities for nicotinic ligands. The crystal structure of AChBP from Aplysia californica in the apo form reveals a more open loop C and distinctive positions for other surface loops, compared with previous structures. Analysis of Aplysia AChBP complexes with nicotinic ligands shows that loop C, which does not significantly change conformation upon binding of the antagonist, methyllycaconitine, further opens to accommodate the peptidic antagonist, alpha-conotoxin ImI, but wraps around the agonists lobeline and epibatidine. The structures also reveal extended and nonoverlapping interaction surfaces for the two antagonists, outside the binding loci for agonists. This comprehensive set of structures reflects a dynamic template for delineating further conformational changes of the LBD of the nicotinic receptor.


==About this Structure==
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations.,Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y EMBO J. 2005 Oct 19;24(20):3635-46. Epub 2005 Sep 29. PMID:16193063<ref>PMID:16193063</ref>
2BYS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica] with <scene name='pdbligand=LOB:'>LOB</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Lob+Binding+Site+For+Chain+J'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BYS OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations., Hansen SB, Sulzenbacher G, Huxford T, Marchot P, Taylor P, Bourne Y, EMBO J. 2005 Oct 19;24(20):3635-46. Epub 2005 Sep 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16193063 16193063]
</div>
<div class="pdbe-citations 2bys" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aplysia californica]]
[[Category: Aplysia californica]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bourne, Y.]]
[[Category: Bourne Y]]
[[Category: Hansen, S.B.]]
[[Category: Hansen SB]]
[[Category: Huxford, T.]]
[[Category: Huxford T]]
[[Category: Marchot, P.]]
[[Category: Marchot P]]
[[Category: Sulzenbacher, G.]]
[[Category: Sulzenbacher G]]
[[Category: Taylor, P.]]
[[Category: Taylor P]]
[[Category: LOB]]
[[Category: acetylcholine binding protein]]
[[Category: conformational flexibility]]
[[Category: lobeline]]
[[Category: nicotinic acetylcholine]]
[[Category: receptor]]
 
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