Conformational features of the C-terminal carboxyamidated pentadecapeptide of CCK ðS19HRISDRD½SO4–YMGWMDF33– NH2Þ were determined by NMR spectroscopy in a zwitterionic membrane-mimetic solvent system, composed of DPC micelles. The C-terminal octapeptide consisted of a well-defined pseudohelix that was nearly identical to the structure previously reported for nonsulfated CCK-8 in the same solvent system. N-terminal amino acids of CCK-15 were highly disordered, with no clear conformational preference. Extensive NOE-restrained molecular dynamics simulations of the CCK-15/CCK1–R complex suggested that almost all the experimentally determined intermolecular contact points provided by NMR, site-directed mutagenesis, and photoaffinity labeling could be simultaneously satisfied, when the N-terminus of the ligand is placed in close spatial proximity to the N-terminus of the receptor.
Molecular Modeling Studies of Sulfated Cholecystokinin-15 / C. GIRAGOSSIAN; S. STONE; A.M. PAPINI; L. MORODER; D. MIERKE. - In: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS. - ISSN 0006-291X. - STAMPA. - 293:(2002), pp. 1053-1059.
Molecular Modeling Studies of Sulfated Cholecystokinin-15
PAPINI, ANNA MARIA;
2002
Abstract
Conformational features of the C-terminal carboxyamidated pentadecapeptide of CCK ðS19HRISDRD½SO4–YMGWMDF33– NH2Þ were determined by NMR spectroscopy in a zwitterionic membrane-mimetic solvent system, composed of DPC micelles. The C-terminal octapeptide consisted of a well-defined pseudohelix that was nearly identical to the structure previously reported for nonsulfated CCK-8 in the same solvent system. N-terminal amino acids of CCK-15 were highly disordered, with no clear conformational preference. Extensive NOE-restrained molecular dynamics simulations of the CCK-15/CCK1–R complex suggested that almost all the experimentally determined intermolecular contact points provided by NMR, site-directed mutagenesis, and photoaffinity labeling could be simultaneously satisfied, when the N-terminus of the ligand is placed in close spatial proximity to the N-terminus of the receptor.File | Dimensione | Formato | |
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