Conformational studies on the pancreatic polypeptide hormone family

Eur J Biochem. 1984 Jul 16;142(2):379-85. doi: 10.1111/j.1432-1033.1984.tb08298.x.

Abstract

Pancreatic polypeptide has been extracted and sequenced from a wide range of species. The 36-residue polypeptides have some hormonal characteristics, and show a high degree of sequence homology. Two recently isolated polypeptides, from porcine gut and brain, also show a high degree of sequence homology with the pancreatic polypeptides. It was proposed that these polypeptides were members of a related family. The X-ray determined structure of one member of the family, turkey pancreatic polypeptide, is known to high resolution, but there is no structural information for the others. Studies designed to give an insight into the tertiary structure of these related molecules have been carried out, including model building using interactive computer graphics, circular dichroic spectroscopy and secondary structure prediction using a variety of algorithms. The results indicate that a compact globular conformation, similar to that observed in turkey pancreatic polypeptide may be adopted by all molecules and that this may be more highly conserved than the individual amino acid sequences.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chemical Phenomena
  • Chemistry, Physical
  • Circular Dichroism
  • Humans
  • Macromolecular Substances
  • Models, Molecular
  • Pancreatic Polypeptide*
  • Protein Conformation
  • Spectrophotometry, Ultraviolet
  • Turkeys*

Substances

  • Macromolecular Substances
  • Pancreatic Polypeptide