1ux2: Difference between revisions

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-[[Image:1ux2.png|left|200px]]
-<!--
+==X-ray structure of acetylcholine binding protein (AChBP)==
-The line below this paragraph, containing "STRUCTURE_1ux2", creates the "Structure Box" on the page.
+<StructureSection load='1ux2' size='340' side='right'caption='[[1ux2]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ux2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UX2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1ux2|  PDB=1ux2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ux2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ux2 OCA], [https://pdbe.org/1ux2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ux2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ux2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ux2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST] Binds to acetylcholine. Modulates neuronal synaptic transmission.
+== 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/ux/1ux2_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=1ux2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nicotinic acetylcholine receptors are prototypes for the pharmaceutically important family of pentameric ligand-gated ion channels. Here we present atomic resolution structures of nicotine and carbamylcholine binding to AChBP, a water-soluble homolog of the ligand binding domain of nicotinic receptors and their family members, GABAA, GABAC, 5HT3 serotonin, and glycine receptors. Ligand binding is driven by enthalpy and is accompanied by conformational changes in the ligand binding site. Residues in the binding site contract around the ligand, with the largest movement in the C loop. As expected, the binding is characterized by substantial aromatic and hydrophobic contributions, but additionally there are close contacts between protein oxygens and positively charged groups in the ligands. The higher affinity of nicotine is due to a main chain hydrogen bond with the B loop and a closer packing of the aromatic groups. These structures will be useful tools for the development of new drugs involving nicotinic acetylcholine receptor-associated diseases.
-===X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP)===
+Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures.,Celie PH, van Rossum-Fikkert SE, van Dijk WJ, Brejc K, Smit AB, Sixma TK Neuron. 2004 Mar 25;41(6):907-14. PMID:15046723<ref>PMID:15046723</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15046723}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1ux2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15046723 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_15046723}}
-==About this Structure==
-[[1ux2]] is a 10 chain structure of [[Acetylcholine binding protein]] with sequence from [http://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UX2 OCA].
 ==See Also==
-*[[Acetylcholine binding protein]]
+*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015046723</ref><ref group="xtra">PMID:011357122</ref><ref group="xtra">PMID:011357121</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Lymnaea stagnalis]]
-[[Category: Brejc, K.]]
+[[Category: Brejc K]]
-[[Category: Celie, P H.N.]]
+[[Category: Celie PHN]]
-[[Category: Dijk, W J.Van.]]
+[[Category: Sixma TK]]
-[[Category: Rossum-Fikkert, S E.Van.]]
+[[Category: Smit AB]]
-[[Category: Sixma, T K.]]
+[[Category: Van Dijk WJ]]
-[[Category: Smit, A B.]]
+[[Category: Van Rossum-fikkert SE]]
-[[Category: Acetylcholine]]
-[[Category: Glycoprotein]]
-[[Category: Igg fold]]
-[[Category: Nicotine]]
-[[Category: Pentamer]]