NMR Studies of Neurotoxin II Spatial Structure

Pashkov, V. S.; Arseniev, Alexander S.; Kondakov, V. I.

doi:10.1007/978-3-642-81344-3_480

Cited by 3 publications

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“…9. The,folding of the short-chain neurotoxin molecule [ I 7,181 according to the N M R data [10][11][12][13][14][15][16][17][18][19][20][21][22][23] and this study. Solid arrows indicate contacts between the amino acid residues directly revealed in the present study.…”

Section: Resultsmentioning

confidence: 99%

“…From the data of Tables 1 and 5 it follows that this CH3 group is in the vicinity of the His-4 imidazole ring (p& 5.96). It was shown earlier that the His-4 imidazole ring of the N.n.oxiana neurotoxin I1 [14], the N. m. mossambica neurotoxin I [21] and the N. n. atra cobrotoxin [22,23] is close to the CH3 group of one of the threonine residues. Comparison of the amino acid sequences (Fig.…”

Section: The Alanine and Threonine Residuesmentioning

confidence: 96%

“…A similar broad and unusually high-field signal with similar characteristic pH dependence was observed in the spectra of homologous neurotoxins: the N . n. oxiana neurotoxin I1 [14] and the N . m. mossambica neurotoxin I [21].…”

Section: Arginine 36mentioning

confidence: 99%

“…The existence of a common conformational type for the short-chain neurotoxins has also been confirmed by NMR studies on the members of the homologous series including neurotoxin I1 of N . n. oxiuna [10,11,[13][14][15][16][17][18], a-toxin of Naja nigricollis [12], cobrotoxin of Naja nuja atra [22,23] …”

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confidence: 99%

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The 1H Nuclear-Magnetic-Resonance Spectra and Spatial Structure of the Naja mossambica mossambica Neurotoxin III

Arseniev¹,

Pashkov²,

Pluzhnikov³

et al. 1981

Eur J Biochem

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The proton NMR spectra at 300 MHz of neurotoxin 111 from venom of Naju mossumbicu mossamhicu are reported. By the use of double resonance techniques, pH dependence chemical shifts, isotope labeling technique, and comparison with homologous neurotoxins all proton signals in the aromatic and methyl regions as well as E -C H~ proton signals of some lysine residues have been assigned to individual amino acid residues and their spatial microenvironment has been determined. The results deduced on the solution structure of neurotoxin I11 are in complete agreement with the crystal structure of sea snake erabutoxins as well as with the previously established backbone folding and inter-residue interactions for the Naju naja oxiana short-chain neurotoxin in solution. In addition evidence has been obtained (a) that the conformation of the p turn in the 31 -34 segment depends on the ionization state of the Asp-31 and His-32 side chain groups and (b) that an intricate electrostatic interaction exists in a system of ionogenic groups of the invariant Lys-27, Lys-47, Asp-31, Arg-33, Glu-38 and His-32 residues. These aspects of dynamic conformation are related to an interaction mechanism of a neurotoxin molecule and a nicotinic acetylcholine receptor.Polypeptide toxins are useful probes for studying neuroconductivity processes on the molecular level. Particular attention is being allotted to toxins of sea and amphibious snakes, blocking transmission of the nerve impulse by specifically binding to the acetylcholine receptor of the postsynaptic membrane [I -31.At present the amino acid sequence of about 30 so-called short-chain neurotoxins (60 -62 amino acid residues with four disulphide bonds) from snake venoms has been determined [4]. A crystal structure is determined for two members of this neurotoxin group, erabutoxin a and b of Laticaudu semifasciala [5,6]. The solution conformation of short-chain neurotoxins is being intensively investigated by various physicochemical methods [7-91. Of these the most informative has proved to be NMR spectroscopy in combination with selective chemical modification [lo-221 so as to insert reporter groups into given sites of the protein molecule. Such an approach has made possible determination of the solution conformation of the central loop (residues 23 -38) of the Naja nu@ oxiana neurotoxin I1 [14-181.The absence of suitable reporter groups for the other parts of the molecule and the difficulty of inserting such groups in these parts had been a stumbling block to their NMR conformational characterization. However, molecules with natural reporter groups in the segments of interest could be selected from the extensive homologous series of the 'short' neurotoxin molecules. In particular several such convenient reporter natural ainino acid residues are to be found in the pertinent segments of the Nuju mossambica mossambica neurotoxin I11 molecule (Fig. 1) which we have studied.Of course, making use of the data obtained from the other members of the homologous neurotoxins is possible under the pro...

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