1rgj: Difference between revisions

Revision as of 15:50, 21 February 2008

NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN AND MIMOTOPE OF THE NICOTINIC ACETILCHOLINE RECEPTOR WITH ENHANCED ACTIVITY

OverviewOverview

The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several methods and a wealth of functional, kinetic and structural data are available. Hence, this system represents a suitable model to explore in detail the dynamics of a peptide-protein interaction. Here, the solution structure of a new complex of the protein toxin with a tridecapeptide ligand exhibiting high affinity has been determined by NMR. As observed for three other previously reported mimotope-alpha-bungarotoxin complexes, also in this case correlations between biological activity and kinetic data are not fully consistent with a static discussion of structural data. Molecular dynamics simulations of the four mimotope-toxin complexes indicate that a relevant contribution to the complex stability is given by the extent of the residual flexibility that the protein maintains upon peptide binding. This feature, limiting the entropy loss caused by protein folding and binding, ought to be generally considered in a rational design of specific protein ligands.

About this StructureAbout this Structure

1RGJ is a Single protein structure of sequence from Bungarus multicinctus. This structure supersedes the now removed PDB entry 1P67. Full crystallographic information is available from OCA.

ReferenceReference

NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin., Bernini A, Ciutti A, Spiga O, Scarselli M, Klein S, Vannetti S, Bracci L, Lozzi L, Lelli B, Falciani C, Neri P, Niccolai N, J Mol Biol. 2004 Jun 18;339(5):1169-77. PMID:15178256

Page seeded by OCA on Thu Feb 21 14:50:39 2008

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

OCA

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-[[Image:1rgj.gif|left|200px]]<br /><applet load="1rgj" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1rgj.gif|left|200px]]<br /><applet load="1rgj" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1rgj" />
 '''NMR STRUCTURE OF THE COMPLEX BETWEEN ALPHA-BUNGAROTOXIN AND MIMOTOPE OF THE NICOTINIC ACETILCHOLINE RECEPTOR WITH ENHANCED ACTIVITY'''<br />
 ==Overview==
-The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been, characterised extensively by several methods and a wealth of functional, kinetic and structural data are available. Hence, this system represents a, suitable model to explore in detail the dynamics of a peptide-protein, interaction. Here, the solution structure of a new complex of the protein, toxin with a tridecapeptide ligand exhibiting high affinity has been, determined by NMR. As observed for three other previously reported, mimotope-alpha-bungarotoxin complexes, also in this case correlations, between biological activity and kinetic data are not fully consistent with, a static discussion of structural data. Molecular dynamics simulations of, the four mimotope-toxin complexes indicate that a relevant contribution to, the complex stability is given by the extent of the residual flexibility, that the protein maintains upon peptide binding. This feature, limiting, the entropy loss caused by protein folding and binding, ought to be, generally considered in a rational design of specific protein ligands.
+The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several methods and a wealth of functional, kinetic and structural data are available. Hence, this system represents a suitable model to explore in detail the dynamics of a peptide-protein interaction. Here, the solution structure of a new complex of the protein toxin with a tridecapeptide ligand exhibiting high affinity has been determined by NMR. As observed for three other previously reported mimotope-alpha-bungarotoxin complexes, also in this case correlations between biological activity and kinetic data are not fully consistent with a static discussion of structural data. Molecular dynamics simulations of the four mimotope-toxin complexes indicate that a relevant contribution to the complex stability is given by the extent of the residual flexibility that the protein maintains upon peptide binding. This feature, limiting the entropy loss caused by protein folding and binding, ought to be generally considered in a rational design of specific protein ligands.
 ==About this Structure==
-RGJ 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 1P67. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RGJ OCA].
+RGJ 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 supersedes the now removed PDB entry 1P67. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RGJ OCA].
 ==Reference==
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 [[Category: protein-peptide complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:34:49 2007''
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