Conformation of the C-terminal pentapeptide—the ‘message sequence’—of tachykinins as determined by consensus dynamic.
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Date
1997-06
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Abstract
The tachykinins are a family of gastrointestinal peptides comprising eight members:
substance P, neurokinin A, neurokinin Β, eledoisin, physalemin, uperolein, kassinin and phyllomedusin.
Consensus dynamics was carried out on an ensemble of seven tachykinins to determine the
binding conformation of the common C-terminal fragment: Phe-X-Gly-Leu-Met-NH2, the ‘message
sequence’ of tachykinins. Three binding modes for the C-terminal pentapeptide were determined. The
first binding conformation is folded due to an intramolecular Η-bond between the NH of the variable
residue (X) and CO of Met. Other features include γ-bends at both the variable amino acid (X) and at
Gly. The global minimum of the simulation has this conformation for the C-terminal pentapeptide.
The other two binding modes have slightly higher energies. The second is chiefly characterized by
a β-turn around the segment X-Gly-Leu-Met, with additional γ-bends at the variable amino acid (X)
and Met. The final binding conformation is composed of γ-bends around the variable amino acid (X)
and Leu, and a ‘pseudo’ γ-bend at the terminal Met.
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Keywords
Tachykinins, conformation, message sequence, consensus dynamics, binding modes
Citation
Kamath Shantaram, Coutinho Evans. Conformation of the C-terminal pentapeptide—the ‘message sequence’—of tachykinins as determined by consensus dynamic. Journal of Biosciences. 1997 Jun; 22(3): 315-324.