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1fra

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(New page: 200px<br /><applet load="1fra" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fra" /> '''TERTIARY STRUCTURE OF ERABUTOXIN B IN AQUEOU...)
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[[Image:1fra.gif|left|200px]]<br /><applet load="1fra" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1fra" />
 
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'''TERTIARY STRUCTURE OF ERABUTOXIN B IN AQUEOUS SOLUTION ELUCIDATED BY TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE'''<br />
 
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==Overview==
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==TERTIARY STRUCTURE OF ERABUTOXIN B IN AQUEOUS SOLUTION ELUCIDATED BY TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE==
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The three-dimensional structure of erabutoxin b, a short-chain neurotoxic, peptide purified from the venom of the sea snake Laticauda semifasciata, was determined in aqueous solution by two-dimensional proton nuclear, magnetic resonance and simulated annealing-based calculations. On the, basis of 883 assigned nuclear Overhauser effect (NOE) connectivities, 676, final distance constraints were derived and used together with 38 torsion, angle (phi, chi 1) constraints, four distance constraints derived from, disulfide bridges and 30 distance constraints derived from hydrogen bonds., A total of 14 converged structures were obtained from 50 runs of, calculations. The atomic root-mean-square difference about the mean, coordinate positions (excluding the residues 18 to 22) is 0.60 A for, backbone atoms (N, C alpha and C'). The protein consists of a core region, from which three finger-like loops emerge outwards. It includes a short, two-stranded antiparallel beta-sheet of residues 2 to 5 and 13 to 16, a, three-stranded antiparallel beta-sheet involving residues 23 to 30, 35 to, 41 and 50 to 56, and four disulfide bridges in the core region. Comparison, with two crystal structures of erabutoxin b at 1.4 A and 1.7 A resolution, indicated that the solution and the crystal structures were very similar, but less defined regions were observed at the localized region of the tip, of the central loop and the outside of the third loop in solution. Other, short-chain alpha-neurotoxins showed structural characteristics similar to, those of erabutoxin b.
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<StructureSection load='1fra' size='340' side='right'caption='[[1fra]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1fra]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FRA FirstGlance]. <br>
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1FRA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Laticauda_semifasciata Laticauda semifasciata]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRA OCA].
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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</td></tr>
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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=1fra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fra OCA], [https://pdbe.org/1fra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fra RCSB], [https://www.ebi.ac.uk/pdbsum/1fra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fra ProSAT]</span></td></tr>
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==Reference==
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</table>
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Tertiary structure of erabutoxin b in aqueous solution as elucidated by two-dimensional nuclear magnetic resonance., Hatanaka H, Oka M, Kohda D, Tate S, Suda A, Tamiya N, Inagaki F, J Mol Biol. 1994 Jul 8;240(2):155-66. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8027999 8027999]
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== Function ==
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[https://www.uniprot.org/uniprot/3S1EB_LATSE 3S1EB_LATSE] Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) (tested on Torpedo marmorata, Kd=0.07 nM), and with low affinity to neuronal alpha-7/CHRNA7 nAChRs (tested on chimeric alpha-7/CHRNA7, Kd=22 uM) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission (PubMed:7721859). Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site.<ref>PMID:9305882</ref>
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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/fr/1fra_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=1fra ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Laticauda semifasciata]]
[[Category: Laticauda semifasciata]]
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[[Category: Single protein]]
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[[Category: Hatanaka H]]
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[[Category: Hatanaka, H.]]
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[[Category: Inagaki F]]
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[[Category: Inagaki, F.]]
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[[Category: Kohda D]]
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[[Category: Kohda, D.]]
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[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:11:07 2007''
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Current revision

TERTIARY STRUCTURE OF ERABUTOXIN B IN AQUEOUS SOLUTION ELUCIDATED BY TWO-DIMENSIONAL NUCLEAR MAGNETIC RESONANCE

PDB ID 1fra

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