1lk1

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1lk1.png|left|200px]]
 
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==MODEL OF THE ACETYLCHOLINE RECEPTOR EXTRACELLULAR DOMAIN IN COMPLEX WITH TWO ALPHA-BUNGAROTOXIN MOLECULES==
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The line below this paragraph, containing "STRUCTURE_1lk1", creates the "Structure Box" on the page.
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<StructureSection load='1lk1' size='340' side='right'caption='[[1lk1]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LK1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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=1lk1 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1lk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lk1 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1lk1| PDB=1lk1 | SCENE= }}
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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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===MODEL OF THE ACETYLCHOLINE RECEPTOR EXTRACELLULAR DOMAIN IN COMPLEX WITH TWO ALPHA-BUNGAROTOXIN MOLECULES===
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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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The line below this paragraph, {{ABSTRACT_PUBMED_12160749}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1lk1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 12160749 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_12160749}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LK1 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:12160749</ref><references group="xtra"/>
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[[Category: Anglister, J]]
[[Category: Anglister, J]]
[[Category: Chill, J]]
[[Category: Chill, J]]
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[[Category: Samson, A O]]
[[Category: Samson, A O]]
[[Category: Scherf, T]]
[[Category: Scherf, T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 09:25:03 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

MODEL OF THE ACETYLCHOLINE RECEPTOR EXTRACELLULAR DOMAIN IN COMPLEX WITH TWO ALPHA-BUNGAROTOXIN MOLECULES

PDB ID 1lk1

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