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New page: left|200px<br /><applet load="2nbt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nbt" /> '''NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES'''...
 
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[[Image:2nbt.jpg|left|200px]]<br /><applet load="2nbt" size="450" color="white" frame="true" align="right" spinBox="true"
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'''NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES'''<br />


==Overview==
==NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES==
Neuronal bungarotoxin has previously been shown, using two-dimensional 1H, NMR spectroscopy, to have a triple-stranded antiparallel beta-sheet, structure which dimerizes in solution [Oswald, R.E., Sutcliffe, M.J., Bamberger, M., Loring, R.H., Braswell, E., &amp; Dobson, C.M. (1991), Biochemistry 30, 4901-4909]. In this paper, structural calculations are, described which use the 582 experimentally measured NOE restraints in, conjunction with 27 phi-angle restraints from J-value measurements. The, positions of the N-terminal region and C-terminal region were poorly, defined in the calculated structures with respect to the remainder of the, structure. The region of the structure containing the triple-stranded, beta-sheet was, however, well defined and similar to that found in the, structure of homologous alpha-bungarotoxin (45% amino acid identity). The, experimental restraints did not result in a well-defined dimer interface, region because of the small number of NOEs which could be identified in, this region. An approach was therefore adopted which produced model, structures based to varying degrees on the alpha-bungarotoxin structure., Fourteen different structures were generated in this manner and, subsequently used as starting points for refinement using dynamical, simulated annealing followed by restrained molecular dynamics. This, approach, which combines NMR data and homologous model building, has, enabled a family of structures to be proposed for the dimeric molecule. In, particular, Phe49 has been identified as possibly playing an important, role in dimer formation, this residue in one chain interacting with the, corresponding residue in the adjacent chain.
<StructureSection load='2nbt' size='340' side='right'caption='[[2nbt]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2nbt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1nbt 1nbt]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NBT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NBT FirstGlance]. <br>
</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=2nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nbt OCA], [https://pdbe.org/2nbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nbt RCSB], [https://www.ebi.ac.uk/pdbsum/2nbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nbt ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/NXL1_BUNMU NXL1_BUNMU]] Neurotoxin. Binds and inhibits nicotinic acetylcholine receptors. Compared to alpha-neurotoxins, kappa-neurotoxins bind more strongly to neuronal receptors, and less strongly to muscle receptors.<ref>PMID:3986193</ref> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nb/2nbt_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2nbt ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Neuronal bungarotoxin has previously been shown, using two-dimensional 1H NMR spectroscopy, to have a triple-stranded antiparallel beta-sheet structure which dimerizes in solution [Oswald, R.E., Sutcliffe, M.J., Bamberger, M., Loring, R.H., Braswell, E., &amp; Dobson, C.M. (1991) Biochemistry 30, 4901-4909]. In this paper, structural calculations are described which use the 582 experimentally measured NOE restraints in conjunction with 27 phi-angle restraints from J-value measurements. The positions of the N-terminal region and C-terminal region were poorly defined in the calculated structures with respect to the remainder of the structure. The region of the structure containing the triple-stranded beta-sheet was, however, well defined and similar to that found in the structure of homologous alpha-bungarotoxin (45% amino acid identity). The experimental restraints did not result in a well-defined dimer interface region because of the small number of NOEs which could be identified in this region. An approach was therefore adopted which produced model structures based to varying degrees on the alpha-bungarotoxin structure. Fourteen different structures were generated in this manner and subsequently used as starting points for refinement using dynamical simulated annealing followed by restrained molecular dynamics. This approach, which combines NMR data and homologous model building, has enabled a family of structures to be proposed for the dimeric molecule. In particular, Phe49 has been identified as possibly playing an important role in dimer formation, this residue in one chain interacting with the corresponding residue in the adjacent chain.


==About this Structure==
Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics.,Sutcliffe MJ, Dobson CM, Oswald RE Biochemistry. 1992 Mar 24;31(11):2962-70. PMID:1550821<ref>PMID:1550821</ref>
2NBT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bungarus_multicinctus Bungarus multicinctus]. This structure superseeds the now removed PDB entry 1NBT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NBT OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics., Sutcliffe MJ, Dobson CM, Oswald RE, Biochemistry. 1992 Mar 24;31(11):2962-70. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1550821 1550821]
</div>
<div class="pdbe-citations 2nbt" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Bungarotoxin 3D structures|Bungarotoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bungarus multicinctus]]
[[Category: Bungarus multicinctus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bamberger, M.]]
[[Category: Bamberger, M]]
[[Category: Braswell, E.]]
[[Category: Braswell, E]]
[[Category: Dobson, C.M.]]
[[Category: Dobson, C M]]
[[Category: Loring, R.H.]]
[[Category: Loring, R H]]
[[Category: Oswald, R.E.]]
[[Category: Oswald, R E]]
[[Category: Sutcliffe, M.J.]]
[[Category: Sutcliffe, M J]]
[[Category: neurotoxin]]
[[Category: Neurotoxin]]
[[Category: toxin]]
[[Category: Toxin]]
[[Category: venom]]
[[Category: Venom]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:46:52 2007''

Latest revision as of 12:06, 23 February 2022

NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURESNEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES

Structural highlights

2nbt is a 2 chain structure with sequence from Bungarus multicinctus. This structure supersedes the now removed PDB entry 1nbt. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NXL1_BUNMU] Neurotoxin. Binds and inhibits nicotinic acetylcholine receptors. Compared to alpha-neurotoxins, kappa-neurotoxins bind more strongly to neuronal receptors, and less strongly to muscle receptors.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Neuronal bungarotoxin has previously been shown, using two-dimensional 1H NMR spectroscopy, to have a triple-stranded antiparallel beta-sheet structure which dimerizes in solution [Oswald, R.E., Sutcliffe, M.J., Bamberger, M., Loring, R.H., Braswell, E., & Dobson, C.M. (1991) Biochemistry 30, 4901-4909]. In this paper, structural calculations are described which use the 582 experimentally measured NOE restraints in conjunction with 27 phi-angle restraints from J-value measurements. The positions of the N-terminal region and C-terminal region were poorly defined in the calculated structures with respect to the remainder of the structure. The region of the structure containing the triple-stranded beta-sheet was, however, well defined and similar to that found in the structure of homologous alpha-bungarotoxin (45% amino acid identity). The experimental restraints did not result in a well-defined dimer interface region because of the small number of NOEs which could be identified in this region. An approach was therefore adopted which produced model structures based to varying degrees on the alpha-bungarotoxin structure. Fourteen different structures were generated in this manner and subsequently used as starting points for refinement using dynamical simulated annealing followed by restrained molecular dynamics. This approach, which combines NMR data and homologous model building, has enabled a family of structures to be proposed for the dimeric molecule. In particular, Phe49 has been identified as possibly playing an important role in dimer formation, this residue in one chain interacting with the corresponding residue in the adjacent chain.

Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics.,Sutcliffe MJ, Dobson CM, Oswald RE Biochemistry. 1992 Mar 24;31(11):2962-70. PMID:1550821[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Grant GA, Chiappinelli VA. kappa-Bungarotoxin: complete amino acid sequence of a neuronal nicotinic receptor probe. Biochemistry. 1985 Mar 12;24(6):1532-7. PMID:3986193
  2. ↑ Sutcliffe MJ, Dobson CM, Oswald RE. Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics. Biochemistry. 1992 Mar 24;31(11):2962-70. PMID:1550821
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