5obg
From Proteopedia
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==Crystal structure of glycine binding protein in complex with strychnine== | ==Crystal structure of glycine binding protein in complex with strychnine== | ||
| - | <StructureSection load='5obg' size='340' side='right' caption='[[5obg]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5obg' size='340' side='right'caption='[[5obg]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5obg]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OBG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5obg]] is a 5 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=5OBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OBG FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SY9:STRYCHNINE'>SY9</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5obg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5obg OCA], [http://pdbe.org/5obg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5obg RCSB], [http://www.ebi.ac.uk/pdbsum/5obg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5obg ProSAT]</span></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=5obg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5obg OCA], [http://pdbe.org/5obg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5obg RCSB], [http://www.ebi.ac.uk/pdbsum/5obg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5obg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5obg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Aplca]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Dawson, A]] | [[Category: Dawson, A]] | ||
[[Category: Hunter, W N]] | [[Category: Hunter, W N]] | ||
Revision as of 04:34, 13 February 2020
Crystal structure of glycine binding protein in complex with strychnine
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