The crystal structures of the synthetic C-terminal octa- and dodecapeptides of trichovirin.
The structures of two synthetic peptides with sequences corresponding to the C-terminal region of the naturally occurring 14-residue peptaibol trichovirin have been determined. The crystal structures of 8- and 12-residue segments are presented and are compared with the structures of the tetrapeptide and of the 9-residue segment, which have been reported earlier. A comparison between these segments leads to the hypothesis that the three-dimensional structure of trichovirin is to a large extent determined by the properties of a periodically repeating -Aib-Pro- pattern in the sequence of the peptide.
Gessmann
R
R
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Crete, Greece.
Benos
P
P
Brückner
H
H
Kokkinidis
M
M
D000595:Amino Acid Sequence; D000621:Aminoisobutyric Acids / Q000737:chemistry; D000900:Anti-Bacterial Agents / Q000138:chemical synthesis / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015394:Molecular Structure; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D010455:Peptides; D011487:Protein Conformation
D000621:Aminoisobutyric Acids; D000900:Anti-Bacterial Agents; D010446:Peptide Fragments; D010455:Peptides; C119176:trichovirin I-4A; C100049:2-aminoisobutyric acid