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New page: left|200px<br /> <applet load="2bj0" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bj0, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O... |
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== | ==Crystal Structure of AChBP from Bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors== | ||
The crystal structure of acetylcholine-binding protein (AChBP) from the | <StructureSection load='2bj0' size='340' side='right'caption='[[2bj0]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bj0]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bulinus_truncatus Bulinus truncatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BJ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BJ0 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CXS:3-CYCLOHEXYL-1-PROPYLSULFONIC+ACID'>CXS</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=2bj0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bj0 OCA], [https://pdbe.org/2bj0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bj0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bj0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bj0 ProSAT]</span></td></tr> | |||
</table> | |||
== 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/bj/2bj0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2bj0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of acetylcholine-binding protein (AChBP) from the mollusk Lymnaea stagnalis is the established model for the ligand binding domains of the ligand-gated ion channel family, which includes nicotinic acetylcholine, 5-hydroxytryptamine (5-HT3), gamma-aminobutyric acid (GABA), types A and C, and glycine receptors. Here we present the crystal structure of a remote homolog, AChBP from Bulinus truncatus, which reveals both the conserved structural scaffold and the sites of variation in this receptor family. These include rigid body movements of loops that are close to the transmembrane interface in the receptors and changes in the intermonomer contacts, which alter the pentamer stability drastically. Structural, pharmacological and mutational analysis of both AChBPs shows how 3 amino acid changes in the binding site contribute to a 5-10-fold difference in affinity for nicotinic ligands. Comparison of these structures will be valuable for improving structure-function studies of ligand-gated ion channel receptors, including signal transduction, homology modeling, and drug design. | |||
Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors.,Celie PH, Klaassen RV, van Rossum-Fikkert SE, van Elk R, van Nierop P, Smit AB, Sixma TK J Biol Chem. 2005 Jul 15;280(28):26457-66. Epub 2005 May 16. PMID:15899893<ref>PMID:15899893</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bj0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bulinus truncatus]] | [[Category: Bulinus truncatus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Celie | [[Category: Celie PHN]] | ||
[[Category: Klaassen RV]] | |||
[[Category: Klaassen | [[Category: Sixma TK]] | ||
[[Category: Smit AB]] | |||
[[Category: Van Elk R]] | |||
[[Category: Sixma | [[Category: Van Nierop P]] | ||
[[Category: Smit | [[Category: Van Rossum-Fikkert SE]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 10:46, 23 October 2024
Crystal Structure of AChBP from Bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptorsCrystal Structure of AChBP from Bulinus truncatus revals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of acetylcholine-binding protein (AChBP) from the mollusk Lymnaea stagnalis is the established model for the ligand binding domains of the ligand-gated ion channel family, which includes nicotinic acetylcholine, 5-hydroxytryptamine (5-HT3), gamma-aminobutyric acid (GABA), types A and C, and glycine receptors. Here we present the crystal structure of a remote homolog, AChBP from Bulinus truncatus, which reveals both the conserved structural scaffold and the sites of variation in this receptor family. These include rigid body movements of loops that are close to the transmembrane interface in the receptors and changes in the intermonomer contacts, which alter the pentamer stability drastically. Structural, pharmacological and mutational analysis of both AChBPs shows how 3 amino acid changes in the binding site contribute to a 5-10-fold difference in affinity for nicotinic ligands. Comparison of these structures will be valuable for improving structure-function studies of ligand-gated ion channel receptors, including signal transduction, homology modeling, and drug design. Crystal structure of acetylcholine-binding protein from Bulinus truncatus reveals the conserved structural scaffold and sites of variation in nicotinic acetylcholine receptors.,Celie PH, Klaassen RV, van Rossum-Fikkert SE, van Elk R, van Nierop P, Smit AB, Sixma TK J Biol Chem. 2005 Jul 15;280(28):26457-66. Epub 2005 May 16. PMID:15899893[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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