TY - JOUR
T1 - Solution Structure of PMP-D2, a 35-Residue Peptide Isolated from the Insect Locusta migratoria
AU - Mer, Georges
AU - Kellenberger, Christine
AU - Koehl, Patrice
AU - Stote, Roland
AU - Sorokine, Odile
AU - Van Dorsselaer, Alain
AU - Luu, Bang
AU - Hietter, Hélène
AU - Lefèvre, Jean Frantçois
PY - 1994/12/1
Y1 - 1994/12/1
N2 - 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.
AB - 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.
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U2 - 10.1021/bi00255a021
DO - 10.1021/bi00255a021
M3 - Article
C2 - 7803403
AN - SCOPUS:0028589068
SN - 0006-2960
VL - 33
SP - 15397
EP - 15407
JO - Biochemistry
JF - Biochemistry
IS - 51
ER -