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 Frantçois Lefèvre

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48 Scopus citations


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
Issue number51
StatePublished - Dec 1 1994

ASJC Scopus subject areas

  • Biochemistry


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