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Conformational and molecular modeling studies of sulfated cholecystokinin-15

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78419

Moroder,  L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Giragossian, C., Stone, S., Papini, A. M., Moroder, L., & Mierke, D. F. (2002). Conformational and molecular modeling studies of sulfated cholecystokinin-15. Biochemical and Biophysical Research Communications, 293(3), 1053-1059.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F38-A
Abstract
Conformational features of the C-terminal carboxyamidated pentadecapeptide of CCK ((SHRISDRD)-H-19[SO4]-YMGWMDF(33)-NH2) 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 photo-affinity 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. (C) 2002 Elsevier Science (USA). All rights reserved.