3sio

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<StructureSection load='3sio' size='340' side='right'caption='[[3sio]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
<StructureSection load='3sio' size='340' side='right'caption='[[3sio]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sio]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sio]] 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=3SIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MLK:METHYLLYCACONITINE'>MLK</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2byr|2byr]], [[3sh1|3sh1]], [[3t4m|3t4m]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MLK:METHYLLYCACONITINE'>MLK</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AChBP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6500 APLCA])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sio OCA], [https://pdbe.org/3sio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sio RCSB], [https://www.ebi.ac.uk/pdbsum/3sio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sio ProSAT]</span></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=3sio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sio OCA], [https://pdbe.org/3sio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sio RCSB], [https://www.ebi.ac.uk/pdbsum/3sio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sio ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8WSF8_APLCA Q8WSF8_APLCA]
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Determining the structure of the ligand-binding domain of the nicotinic acetylcholine receptor (nAChR) has been a long standing goal in the design of selective drugs useful in implicated diseases for this prevalent receptor family. Acetylcholine-binding proteins have proven to be valuable surrogates with structural similarity and sequence identity to the extracellular domain of the nicotinic receptor, yet these soluble proteins have their unique features and do not serve as exact replicates of the nAChRs of interest. Here we systematically modify the sequence of these proteins toward the homomeric human alpha7 nAChR. These chimeric proteins exhibit a shift in affinities to reflect alpha7 binding characteristics yet maintain expression levels and stability conducive for crystallization. We also present a pentameric humanoid nAChR extracellular domain with the structural determination of the alpha7 nAChR glycosylation site.
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Creating an alpha7 nicotinic acetylcholine recognition domain from the acetylcholine-binding protein: crystallographic and ligand selectivity analyses.,Nemecz A, Taylor P J Biol Chem. 2011 Dec 9;286(49):42555-65. Epub 2011 Oct 18. PMID:22009746<ref>PMID:22009746</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sio" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aplca]]
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[[Category: Aplysia californica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Nemecz, A]]
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[[Category: Nemecz A]]
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[[Category: Taylor, P W]]
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[[Category: Taylor PW]]
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[[Category: Acetylcholine]]
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[[Category: Achbp]]
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[[Category: Alpha-7 human nicotinic acetylcholine receptor]]
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[[Category: Aplysia californica]]
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[[Category: Binding protein]]
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[[Category: Glycosylation]]
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[[Category: Methyllycaconitine]]
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[[Category: Mutated acetylcholine binding protein]]
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[[Category: Nachr]]
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[[Category: Receptor]]
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Revision as of 06:44, 3 April 2024

Ac-AChBP ligand binding domain (not including beta 9-10 linker) mutated to human alpha-7 nAChR

PDB ID 3sio

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OCA

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