1ljz

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[[Image:1ljz.gif|left|200px]]
 
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{{Structure
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==NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin==
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|PDB= 1ljz |SIZE=350|CAPTION= <scene name='initialview01'>1ljz</scene>
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<StructureSection load='1ljz' size='340' side='right'caption='[[1ljz]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1ljz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus] and [https://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJZ 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">Solution NMR, 19 models</td></tr>
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|GENE=
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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=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [https://pdbe.org/1ljz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB], [https://www.ebi.ac.uk/pdbsum/1ljz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ljz ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1l4w|1l4w]]
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== Evolutionary Conservation ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ljz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljz OCA], [http://www.ebi.ac.uk/pdbsum/1ljz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ljz RCSB]</span>
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[[Image:Consurf_key_small.gif|200px|right]]
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}}
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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/lj/1ljz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ljz 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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The structure of a peptide corresponding to residues 182-202 of the acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin was solved using NMR spectroscopy. The peptide contains the complete sequence of the major determinant of AChR involved in alpha-bungarotoxin binding. One face of the long beta hairpin formed by the AChR peptide consists of exposed nonconserved residues, which interact extensively with the toxin. Mutations of these receptor residues confer resistance to the toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An NMR-derived model for the receptor complex with two alpha-bungarotoxin molecules shows that this pocket is occupied by the conserved alpha-neurotoxin residue R36, which forms cation-pi interactions with both alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine.
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'''NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin'''
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The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR.,Samson A, Scherf T, Eisenstein M, Chill J, Anglister J Neuron. 2002 Jul 18;35(2):319-32. PMID:12160749<ref>PMID:12160749</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 1ljz" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structure of a peptide corresponding to residues 182-202 of the acetylcholine receptor alpha1 subunit in complex with alpha-bungarotoxin was solved using NMR spectroscopy. The peptide contains the complete sequence of the major determinant of AChR involved in alpha-bungarotoxin binding. One face of the long beta hairpin formed by the AChR peptide consists of exposed nonconserved residues, which interact extensively with the toxin. Mutations of these receptor residues confer resistance to the toxin. Conserved AChR residues form the opposite face of the beta hairpin, which creates the inner and partially hidden pocket for acetylcholine. An NMR-derived model for the receptor complex with two alpha-bungarotoxin molecules shows that this pocket is occupied by the conserved alpha-neurotoxin residue R36, which forms cation-pi interactions with both alphaW149 and gammaW55/deltaW57 of the receptor and mimics acetylcholine.
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*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1LJZ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJZ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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The mechanism for acetylcholine receptor inhibition by alpha-neurotoxins and species-specific resistance to alpha-bungarotoxin revealed by NMR., Samson A, Scherf T, Eisenstein M, Chill J, Anglister J, Neuron. 2002 Jul 18;35(2):319-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12160749 12160749]
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[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Anglister, J.]]
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[[Category: Torpedo marmorata]]
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[[Category: Chill, J H.]]
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[[Category: Anglister J]]
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[[Category: Eisenstein, M.]]
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[[Category: Chill JH]]
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[[Category: Samson, A O.]]
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[[Category: Eisenstein M]]
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[[Category: Scherf, T.]]
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[[Category: Samson AO]]
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[[Category: acetylcholine receptor]]
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[[Category: Scherf T]]
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[[Category: beta-hairpin]]
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[[Category: bungarotoxin]]
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[[Category: intermolecular beta-sheet]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:44 2008''
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Current revision

NMR structure of an AChR-peptide (Torpedo Californica, alpha-subunit residues 182-202) in complex with alpha-Bungarotoxin

PDB ID 1ljz

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