5oaj: Difference between revisions

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 ==Crystal structure of mutant AChBP in complex with tropisetron (T53F, Q74R, Y110A, I135S, G162E)==
-<StructureSection load='5oaj' size='340' side='right' caption='[[5oaj]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
+<StructureSection load='5oaj' size='340' side='right'caption='[[5oaj]], [[Resolution|resolution]] 2.47&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5oaj]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Aplca Aplca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OAJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OAJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5oaj]] 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=5OAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OAJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TKT:(3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL+1H-INDOLE-3-CARBOXYLATE'>TKT</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]] 2.47&#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=5oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oaj OCA], [http://pdbe.org/5oaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oaj RCSB], [http://www.ebi.ac.uk/pdbsum/5oaj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oaj ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=TKT:(3-ENDO)-8-METHYL-8-AZABICYCLO[3.2.1]OCT-3-YL+1H-INDOLE-3-CARBOXYLATE'>TKT</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=5oaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oaj OCA], [https://pdbe.org/5oaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oaj RCSB], [https://www.ebi.ac.uk/pdbsum/5oaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oaj ProSAT]</span></td></tr>
 </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 5oaj" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>
-[[Category: Aplca]]
+[[Category: Aplysia californica]]
-[[Category: Dawson, A]]
+[[Category: Large Structures]]
-[[Category: Hunter, W N]]
+[[Category: Dawson A]]
-[[Category: Souza, J O.de]]
+[[Category: Hunter WN]]
-[[Category: Trumper, P]]
+[[Category: Trumper P]]
-[[Category: Acetylcholine binding]]
+[[Category: De Souza JO]]
-[[Category: Receptor]]
-[[Category: Signaling protein]]