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  • Title: Structure of human calcitonin gene-related peptide (hCGRP) and of its antagonist hCGRP 8-37 as determined by NMR and molecular modeling.
    Author: Boulanger Y, Khiat A, Chen Y, Senécal L, Tu Y, St-Pierre S, Fournier A.
    Journal: Pept Res; 1995; 8(4):206-13. PubMed ID: 8527874.
    Abstract:
    The solution structures of human calcitonin gene-related peptide (hCGRP, 37 residues) and of its antagonistic fragment hCGRP 8-37 have been determined by two-dimensional 1H nuclear magnetic resonance (NMR) spectroscopy and molecular modeling. Analysis of the double quantum filtered correlation spectroscopy, total correlation spectroscopy and nuclear Overhauser enhancement spectroscopy spectra led to a complete assignment and to the identification of more than 350 intra- and interresidue connectivities for each peptide. Molecular models were calculated by molecular dynamics and energy minimization using distance constraints. The structure of hCGRP is characterized by a rigid N-terminal disulfide-bonded loop followed by helix segments (Val8-Leu16), a gamma-turn (Ser19-Gly21) and several local hydrogen-bonded patterns. The structure of hCGRP 8-37 is less defined than the structure of hCGRP and no helix structure is present. Molecular models of both peptides are consistent with the NH temperature coefficients and secondary chemical shifts of the alpha-protons. Hydrogen bonding with the disulfide-bonded ring appears to be critical for helix formation, both structural elements being essential for agonistic activity.
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