Spatial organization and conformational peculiarities of the callatostatin family of neuropeptides.
The structures and conformational peculiarities of five members of the callatostatin family of neuropeptides, i.e. Leu- and Met-callatostatins, ranging in size from 8 to 16 amino acid residues have been investigated by a theoretical conformational analysis method. A comparative analysis of the conformational flexibilities of Met-callatostatin with those of the hydroxylated analogues, [Hyp2]- and [Hyp3]-Met-callatostatin has been carried out. Helically packed C-terminal pentapeptide in the structure of all investigated Leu-callatostatins are shown to be possible. The reason for the great number low-energy conformers for the callatostatin N-terminus is discussed.
Alieva
I N
IN
Laboratory of Molecular Biophysics, Baku State University, Azerbaijan Republic.
Velieva
L I
LI
Alie
D I
DI
Godjaev
N M
NM
D000595:Amino Acid Sequence; D000818:Animals; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013816:Thermodynamics
D009479:Neuropeptides; D009842:Oligopeptides; D010446:Peptide Fragments; C080360:callatostatin