This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2nbt

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 23:54, 10 September 2015

NEURONAL 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

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.

References

↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nbt"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2nbt]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nbt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2nbt RCSB], [http://www.ebi.ac.uk/pdbsum/2nbt PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nbt OCA], [http://pdbe.org/2nbt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nbt RCSB], [http://www.ebi.ac.uk/pdbsum/2nbt PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2nbt" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Bungarotoxin|Bungarotoxin]]
 == References ==
 <references/>

2nbt

From Proteopedia

Revision as of 23:54, 10 September 2015

NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox