1uv6

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[[Image:1uv6.gif|left|200px]]
 
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{{Structure
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==X-ray structure of acetylcholine binding protein (AChBP) in complex with carbamylcholine==
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|PDB= 1uv6 |SIZE=350|CAPTION= <scene name='initialview01'>1uv6</scene>, resolution 2.50&Aring;
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<StructureSection load='1uv6' size='340' side='right'caption='[[1uv6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Cce+Binding+Site+For+Chain+J'>AC1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CCE:2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM'>CCE</scene>
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<table><tr><td colspan='2'>[[1uv6]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. The November 2005 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Acetylcholine Receptor'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2005_11 10.2210/rcsb_pdb/mom_2005_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UV6 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCE:2-[(AMINOCARBONYL)OXY]-N,N,N-TRIMETHYLETHANAMINIUM'>CCE</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uv6 OCA], [https://pdbe.org/1uv6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uv6 RCSB], [https://www.ebi.ac.uk/pdbsum/1uv6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uv6 ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uv6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uv6 OCA], [http://www.ebi.ac.uk/pdbsum/1uv6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uv6 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/ACHP_LYMST ACHP_LYMST] Binds to acetylcholine. Modulates neuronal synaptic transmission.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/uv/1uv6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1uv6 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''X-RAY STRUCTURE OF ACETYLCHOLINE BINDING PROTEIN (ACHBP) IN COMPLEX WITH CARBAMYLCHOLINE'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1uv6" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Acetylcholine binding protein 3D structures|Acetylcholine binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1UV6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lymnaea_stagnalis Lymnaea stagnalis]. The following page contains interesting information on the relation of 1UV6 with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb71_1.html Acetylcholine Receptor]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV6 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15046723 15046723]
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[[Category: Acetylcholine Receptor]]
[[Category: Acetylcholine Receptor]]
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[[Category: Large Structures]]
[[Category: Lymnaea stagnalis]]
[[Category: Lymnaea stagnalis]]
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[[Category: Single protein]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Brejc, K.]]
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[[Category: Brejc K]]
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[[Category: Celie, P H.N.]]
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[[Category: Celie PHN]]
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[[Category: Dijk, W J.Van.]]
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[[Category: Sixma TK]]
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[[Category: Rossum-Fikkert, S E.Van.]]
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[[Category: Smit AB]]
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[[Category: Sixma, T K.]]
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[[Category: Van Dijk WJ]]
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[[Category: Smit, A B.]]
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[[Category: Van Rossum-fikkert SE]]
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[[Category: glycoprotein]]
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[[Category: igg fold]]
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[[Category: immunoglobulin domain]]
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[[Category: pentamer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:15:42 2008''
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Current revision

X-ray structure of acetylcholine binding protein (AChBP) in complex with carbamylcholine

PDB ID 1uv6

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