1H nuclear-magnetic-resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins

W. E. Steinmetz, P. E. Bougis, H. Rochat, O. D. Redwine, Werner Braun, K. Wuthrich

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Abstract

Using the previously reported sequence-specific 1H-NMR assignments, structural constraints for the cardiotoxin CTXIIb from Naja mossambica mossambica were collected. These include distance constraints from nuclear Overhauser enhancement measurements both in the laboratory and in the rotating frame, dihedral angle constraints derived from spin-spin coupling constants, and constraints from hydrogen bonds and disulfide bridges. Structure calculations with the distance geometry program DISMAN confirmed the presence of the previously identified antiparallel β-sheets formed by residues 1-5 and 10-14, and by 20-27, 35-39 and 49-55, and established the nature of the connections between the individual β-strands. These include a right-handed crossover between the two peripheral strands in the triple-stranded β-sheet, and a type I tight turn immediately preceding the β-strand 49-55. The spatial arrangement of the polypeptide backbone in the solution strudture of CTXIIb is closely similar to that in the crystal structure of the homologous cardiotoxin V(II)4 from the same species. In an Appendix the origin of the large pH dependence of two amide proton chemical shifts in CTXIIb is explained.

Original languageEnglish (US)
Pages (from-to)101-116
Number of pages16
JournalEuropean Journal of Biochemistry
Volume172
Issue number1
StatePublished - 1988
Externally publishedYes

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Cobra Cardiotoxin Proteins
Cardiotoxins
Elapidae
Chemical shift
Dihedral angle
Amides
Disulfides
Protons
Hydrogen
Hydrogen bonds
Magnetic Resonance Spectroscopy
Crystal structure
Nuclear magnetic resonance
Peptides
Geometry
cardiotoxin V
Proton Magnetic Resonance Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

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abstract = "Using the previously reported sequence-specific 1H-NMR assignments, structural constraints for the cardiotoxin CTXIIb from Naja mossambica mossambica were collected. These include distance constraints from nuclear Overhauser enhancement measurements both in the laboratory and in the rotating frame, dihedral angle constraints derived from spin-spin coupling constants, and constraints from hydrogen bonds and disulfide bridges. Structure calculations with the distance geometry program DISMAN confirmed the presence of the previously identified antiparallel β-sheets formed by residues 1-5 and 10-14, and by 20-27, 35-39 and 49-55, and established the nature of the connections between the individual β-strands. These include a right-handed crossover between the two peripheral strands in the triple-stranded β-sheet, and a type I tight turn immediately preceding the β-strand 49-55. The spatial arrangement of the polypeptide backbone in the solution strudture of CTXIIb is closely similar to that in the crystal structure of the homologous cardiotoxin V(II)4 from the same species. In an Appendix the origin of the large pH dependence of two amide proton chemical shifts in CTXIIb is explained.",
author = "Steinmetz, {W. E.} and Bougis, {P. E.} and H. Rochat and Redwine, {O. D.} and Werner Braun and K. Wuthrich",
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T1 - 1H nuclear-magnetic-resonance studies of the three-dimensional structure of the cardiotoxin CTXIIb from Naja mossambica mossambica in aqueous solution and comparison with the crystal structures of homologous toxins

AU - Steinmetz, W. E.

AU - Bougis, P. E.

AU - Rochat, H.

AU - Redwine, O. D.

AU - Braun, Werner

AU - Wuthrich, K.

PY - 1988

Y1 - 1988

N2 - Using the previously reported sequence-specific 1H-NMR assignments, structural constraints for the cardiotoxin CTXIIb from Naja mossambica mossambica were collected. These include distance constraints from nuclear Overhauser enhancement measurements both in the laboratory and in the rotating frame, dihedral angle constraints derived from spin-spin coupling constants, and constraints from hydrogen bonds and disulfide bridges. Structure calculations with the distance geometry program DISMAN confirmed the presence of the previously identified antiparallel β-sheets formed by residues 1-5 and 10-14, and by 20-27, 35-39 and 49-55, and established the nature of the connections between the individual β-strands. These include a right-handed crossover between the two peripheral strands in the triple-stranded β-sheet, and a type I tight turn immediately preceding the β-strand 49-55. The spatial arrangement of the polypeptide backbone in the solution strudture of CTXIIb is closely similar to that in the crystal structure of the homologous cardiotoxin V(II)4 from the same species. In an Appendix the origin of the large pH dependence of two amide proton chemical shifts in CTXIIb is explained.

AB - Using the previously reported sequence-specific 1H-NMR assignments, structural constraints for the cardiotoxin CTXIIb from Naja mossambica mossambica were collected. These include distance constraints from nuclear Overhauser enhancement measurements both in the laboratory and in the rotating frame, dihedral angle constraints derived from spin-spin coupling constants, and constraints from hydrogen bonds and disulfide bridges. Structure calculations with the distance geometry program DISMAN confirmed the presence of the previously identified antiparallel β-sheets formed by residues 1-5 and 10-14, and by 20-27, 35-39 and 49-55, and established the nature of the connections between the individual β-strands. These include a right-handed crossover between the two peripheral strands in the triple-stranded β-sheet, and a type I tight turn immediately preceding the β-strand 49-55. The spatial arrangement of the polypeptide backbone in the solution strudture of CTXIIb is closely similar to that in the crystal structure of the homologous cardiotoxin V(II)4 from the same species. In an Appendix the origin of the large pH dependence of two amide proton chemical shifts in CTXIIb is explained.

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