Related ArticlesNMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor.
J Biol Chem. 2002 Apr 5;277(14):12406-17
Authors: Moise L, Piserchio A, Basus VJ, Hawrot E
We report a new, higher resolution NMR structure of alpha-bungarotoxin that defines the structure-determining disulfide core and beta-sheet regions. We further report the NMR structure of the stoichiometric complex formed between alpha-bungarotoxin and a recombinantly expressed 19-mer peptide ((178)IPGKRTESFYECCKEPYPD(196)) derived from the alpha7 subunit of the chick neuronal nicotinic acetylcholine receptor. A comparison of these two structures reveals binding-induced stabilization of the flexible tip of finger II in alpha-bungarotoxin. The conformational rearrangements in the toxin create an extensive binding surface involving both sides of the alpha7 19-mer hairpin-like structure. At the contact zone, Ala(7), Ser(9), and Ile(11) in finger I and Arg(36), Lys(38), Val(39), and Val(40) in finger II of alpha-bungarotoxin interface with Phe(186), Tyr(187), Glu(188), and Tyr(194) in the alpha7 19-mer underscoring the importance of receptor aromatic residues as critical neurotoxin-binding determinants. Superimposing the structure of the complex onto that of the acetylcholine-binding protein (1I9B), a soluble homologue of the extracellular domain of the alpha7 receptor, places alpha-bungarotoxin at the peripheral surface of the inter-subunit interface occluding the agonist-binding site. The disulfide-rich core of alpha-bungarotoxin is suggested to be tilted in the direction of the membrane surface with finger II extending into the proposed ligand-binding cavity.
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Visualizing the principal component of 1H,15N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C
Abstract Laboratories often repeatedly determine the structure of a given protein under a variety of conditions, mutations, modifications, or in a number of states. This approach can be cumbersome and tedious. Given then a database of structures, identifiers, and corresponding 1H,15N-HSQC NMR spectra for homologous proteins, we investigated whether structural information could be ascertained for a new homolog solely from its...
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09-30-2011 08:01 PM
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 06:00 AM
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
Visualizing the principal component of (1)H, (15)N-HSQC NMR spectral changes that reflect protein structural or functional properties: application to troponin C.
J Biomol NMR. 2011 Sep;51(1-2):115-22
Authors: Robertson IM, Boyko RF, Sykes BD
Abstract
Laboratories often repeatedly determine the structure of a given protein under a variety of conditions,...
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09-30-2011 05:59 AM
[NMR paper] NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural di
NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
Related Articles NMR analysis of synthetic human serum albumin alpha-helix 28 identifies structural distortion upon amadori modification.
J Biol Chem. 2005 Jun 17;280(24):22582-9
Authors: Howard MJ, Smales CM
The non-enzymatic reaction between reducing sugars and long-lived proteins in vivo results in the formation of glycation and advanced glycation end products, which alter the properties of proteins including charge,...
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11-25-2010 08:21 PM
[NMR paper] NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
Related Articles NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin.
J Mol Biol. 2004 Jun 18;339(5):1169-77
Authors: Bernini A, Ciutti A, Spiga O, Scarselli M, Klein S, Vannetti S, Bracci L, Lozzi L, Lelli B, Falciani C, Neri P, Niccolai N
The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several...
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11-24-2010 09:51 PM
[NMR paper] NMR-based binding screen and structural analysis of the complex formed between alpha-
NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
Related Articles NMR-based binding screen and structural analysis of the complex formed between alpha-cobratoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica.
J Biol Chem. 2002 Oct 4;277(40):37439-45
Authors: Zeng H, Hawrot E
The alpha18-mer...
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11-24-2010 08:58 PM
[NMR paper] NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic ace
NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Related Articles NMR structure of alpha-bungarotoxin free and bound to a mimotope of the nicotinic acetylcholine receptor.
Biochemistry. 2002 Feb 5;41(5):1457-63
Authors: Scarselli M, Spiga O, Ciutti A, Bernini A, Bracci L, Lelli B, Lozzi L, Calamandrei D, Di Maro D, Klein S, Niccolai N
A combinatorial library approach was used to produce synthetic peptides mimicking the snake neurotoxin binding site of nicotinic receptors. Among the...
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11-24-2010 08:49 PM
[NMR paper] Principal components analysis of protein structure ensembles calculated using NMR dat
Principal components analysis of protein structure ensembles calculated using NMR data.
Related Articles Principal components analysis of protein structure ensembles calculated using NMR data.
J Biomol NMR. 2001 May;20(1):61-70
Authors: Howe PW
One important problem when calculating structures of biomolecules from NMR data is distinguishing converged structures from outlier structures. This paper describes how Principal Components Analysis (PCA) has the potential to classify calculated structures automatically, according to correlated...
NMR structural analysis of alpha-bungarotoxin and its complex with the principal alph
Linear Mode
