Conformational study of the threonine-rich C-terminal pentapeptide of peptide T.
The conformation of the synthetic pentapeptide Thr-Thr-Asn-Tyr-Thr, the C-terminal part of peptide T has been studied using 2D NMR experiments. The nuclear Overhauser effects (NOESY) and the low temperature coefficients for two particular NH chemical shifts allow the proposal for two distinct beta-turn arrangements. This conformation is not in accordance with recent reports but is consistent with observed beta-bends in two sequences of ribonuclease A. The semi-rigid conformation found in the pentapeptide in which the hydroxyl groups are exposed at the periphery of the molecule could be a crucial feature to explain the ability of peptide T to bind to a specific receptor and to correlate with the observed biological activity against HIV.
Cotelle
N
N
INSERM U16, Lille, France.
Lohez
M
M
Cotelle
P
P
Hénichart
J P
JP
D000595:Amino Acid Sequence; D000998:Antiviral Agents / Q000494:pharmacology; D006678:HIV / Q000187:drug effects; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides; D015717:Peptide T / Q000494:pharmacology; D011487:Protein Conformation; D013912:Threonine
D000998:Antiviral Agents; D009842:Oligopeptides; D015717:Peptide T; D013912:Threonine