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1coe

From Proteopedia

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[[Image:1coe.gif|left|200px]]<br /><applet load="1coe" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1coe" />
 
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'''SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY'''<br />
 
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==Overview==
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==SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY==
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The solution conformation of cobrotoxin has been determined by using proton nuclear magnetic resonance spectroscopy. With the combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of cobrotoxin was completely assigned (Yu et al., 1990). A set of 435 approximate interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 29 dihedral angle constraints (from coupling constant measurements) and 26 hydrogen bonding restraints (from the pattern of short-range NOEs), form the basis of 3-D structure determination by the hybrid distance geometry-dynamical simulated annealing method. The 23 structures that were obtained satisfy the experimental restraints, display small deviation from idealized covalent geometry, and possess good nonbonded contacts. Analysis of converged structures indicated that there are two antiparallel beta sheets (double and triple stranded), duly confirming our earlier observations. These are well defined in terms of both atomic root mean square (RMS) differences and backbone torsional angles. The average backbone RMS deviation between the calculated structures and the mean structure, for the beta-sheet regions, is 0.92 A. The mean solution structure was compared with the X-ray crystal structure of erabutoxin b, the homologous protein. This yielded information that both structures resemble each other except at the exposed loop/surface regions, where the solution structure seems to possess more flexibility.
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<StructureSection load='1coe' size='340' side='right'caption='[[1coe]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1coe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COE FirstGlance]. <br>
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1COE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COE 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=1coe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coe OCA], [https://pdbe.org/1coe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1coe RCSB], [https://www.ebi.ac.uk/pdbsum/1coe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1coe ProSAT]</span></td></tr>
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==Reference==
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</table>
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Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study., Yu C, Bhaskaran R, Chuang LC, Yang CC, Biochemistry. 1993 Mar 9;32(9):2131-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8443154 8443154]
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== Function ==
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[https://www.uniprot.org/uniprot/3S1CB_NAJAT 3S1CB_NAJAT] Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Has a higher toxicity than cobrotoxin-b.
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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/co/1coe_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=1coe ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Naja atra]]
[[Category: Naja atra]]
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[[Category: Single protein]]
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[[Category: Bhaskaran R]]
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[[Category: Bhaskaran, R.]]
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[[Category: Yang CC]]
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[[Category: Yang, C C.]]
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[[Category: Yu C]]
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[[Category: Yu, C.]]
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[[Category: short neurotoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:08:04 2008''
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Current revision

SOLUTION CONFORMATION OF COBROTOXIN: A NUCLEAR MAGNETIC RESONANCE AND HYBRID DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING STUDY

PDB ID 1coe

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