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==Crystal structure of wild type Aplysia californica AChBP in complex with strychnine==
==Crystal structure of wild type Aplysia californica AChBP in complex with strychnine==
<StructureSection load='5o8t' size='340' side='right' caption='[[5o8t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5o8t' size='340' side='right'caption='[[5o8t]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5o8t]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O8T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O8T FirstGlance]. <br>
<table><tr><td colspan='2'>[[5o8t]] is a 5 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=5O8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O8T FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SY9:STRYCHNINE'>SY9</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=5o8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o8t OCA], [http://pdbe.org/5o8t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o8t RCSB], [http://www.ebi.ac.uk/pdbsum/5o8t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o8t ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SY9:STRYCHNINE'>SY9</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=5o8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o8t OCA], [https://pdbe.org/5o8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o8t RCSB], [https://www.ebi.ac.uk/pdbsum/5o8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o8t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8WSF8_APLCA Q8WSF8_APLCA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protein-engineering methods have been exploited to produce a surrogate system for the extracellular neurotransmitter-binding site of a heteromeric human ligand-gated ion channel, the glycine receptor. This approach circumvents two major issues: the inherent experimental difficulties in working with a membrane-bound ion channel and the complication that a heteromeric assembly is necessary to create a key, physiologically relevant binding site. Residues that form the orthosteric site in a highly stable ortholog, acetylcholine-binding protein, were selected for substitution. Recombinant proteins were prepared and characterized in stepwise fashion exploiting a range of biophysical techniques, including X-ray crystallography, married to the use of selected chemical probes. The decision making and development of the surrogate, which is termed a glycine-binding protein, are described, and comparisons are provided with wild-type and homomeric systems that establish features of molecular recognition in the binding site and the confidence that the system is suited for use in early-stage drug discovery targeting a heteromeric alpha/beta glycine receptor.
Engineering a surrogate human heteromeric alpha/beta glycine receptor orthosteric site exploiting the structural homology and stability of acetylcholine-binding protein.,Dawson A, Trumper P, de Souza JO, Parker H, Jones MJ, Hales TG, Hunter WN IUCrJ. 2019 Sep 4;6(Pt 6):1014-1023. doi: 10.1107/S205225251901114X. eCollection , 2019 Nov 1. PMID:31709057<ref>PMID:31709057</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5o8t" style="background-color:#fffaf0;"></div>
==See Also==
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dawson, A]]
[[Category: Aplysia californica]]
[[Category: Hunter, W N]]
[[Category: Large Structures]]
[[Category: Souza, J O.de]]
[[Category: Dawson A]]
[[Category: Trumper, P]]
[[Category: Hunter WN]]
[[Category: Receptor]]
[[Category: Trumper P]]
[[Category: Signaling protein]]
[[Category: De Souza JO]]

Latest revision as of 09:37, 6 December 2023

Crystal structure of wild type Aplysia californica AChBP in complex with strychnine

5o8t, resolution 2.20Å

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