Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria

Georges Mer, Christine Kellenberger, Patrice Koehl, Roland Stote, Odile Sorokine, Alain Van Dorsselaer, Bang Luu, Hélène Hietter, Jean François Lefèvre

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The three-dimensional solution structure of PMP-D2, a 35 amino acid peptide isolated from the insect Locusta migratoria, has been determined from two-dimensional 1H NMR spectroscopy data. The structure calculations were performed from 222 NOE-derived interproton distances and 11 dihedral angles calculated from the JHN-Hα coupling constants, using either a combination of distance geometry and restrained simulated annealing or by restrained simulated annealing alone. PMP-D2 contains three disulfide bridges that have been assigned from NMR data and structure calculations and independently confirmed using chemical and enzymatic methods. The core region of PMP-D2 adopts a compact globular fold, stabilized by hydrophobic interactions, which consists of a short three-stranded antiparallel β-sheet involving residues 8-11, 15-19. and 25-29. Back-calculation of the NOESY spectra was used to validate the final structures. Analysis of the CD spectra of PMP-D2 under various conditions of ionic strength and in the presence of organic solvents demonstrates the high stability of this molecule. PMP-D2 was recently shown to inhibit Ca2+ currents. This activity is discussed based on the comparison of PMP-D2 three-dimensional structure with the recently established three-dimensional structure of the Ca2+ channel blocker ω-conotoxin GVIA.

Original languageEnglish (US)
Pages (from-to)15397-15407
Number of pages11
JournalBiochemistry
Volume33
Issue number51
StatePublished - 1994
Externally publishedYes

Fingerprint

Conotoxins
Locusta migratoria
Hydrophobic and Hydrophilic Interactions
Disulfides
Osmolar Concentration
Insects
Spectrum Analysis
Magnetic Resonance Spectroscopy
Simulated annealing
Amino Acids
Peptides
Dihedral angle
Ionic strength
Organic solvents
Nuclear magnetic resonance spectroscopy
Nuclear magnetic resonance
Molecules
Geometry
Proton Magnetic Resonance Spectroscopy

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mer, G., Kellenberger, C., Koehl, P., Stote, R., Sorokine, O., Van Dorsselaer, A., ... Lefèvre, J. F. (1994). Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. Biochemistry, 33(51), 15397-15407.

Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. / Mer, Georges; Kellenberger, Christine; Koehl, Patrice; Stote, Roland; Sorokine, Odile; Van Dorsselaer, Alain; Luu, Bang; Hietter, Hélène; Lefèvre, Jean François.

In: Biochemistry, Vol. 33, No. 51, 1994, p. 15397-15407.

Research output: Contribution to journalArticle

Mer, G, Kellenberger, C, Koehl, P, Stote, R, Sorokine, O, Van Dorsselaer, A, Luu, B, Hietter, H & Lefèvre, JF 1994, 'Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria', Biochemistry, vol. 33, no. 51, pp. 15397-15407.
Mer G, Kellenberger C, Koehl P, Stote R, Sorokine O, Van Dorsselaer A et al. Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. Biochemistry. 1994;33(51):15397-15407.
Mer, Georges ; Kellenberger, Christine ; Koehl, Patrice ; Stote, Roland ; Sorokine, Odile ; Van Dorsselaer, Alain ; Luu, Bang ; Hietter, Hélène ; Lefèvre, Jean François. / Solution structure of PMP-D2, a 35-residue peptide isolated from the insect Locusta migratoria. In: Biochemistry. 1994 ; Vol. 33, No. 51. pp. 15397-15407.
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