2nbt: Difference between revisions

Revision as of 15:06, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2nbt.png

Template:STRUCTURE 2nbt

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

Template:ABSTRACT PUBMED 1550821

About this StructureAbout this Structure

2NBT is a Single protein structure of sequence from Bungarus multicinctus. This structure supersedes the now removed PDB entry 1nbt. Full experimental information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES'''
+===NEURONAL BUNGAROTOXIN, NMR, 10 STRUCTURES===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_1550821}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_1550821}}
 ==About this Structure==
-NBT is a [[Single protein]] structure of 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 crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NBT OCA].
+NBT is a [[Single protein]] structure of 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].
 ==Reference==
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 [[Category: Toxin]]
 [[Category: Venom]]
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