Evidence that the PTH receptor binding site on PTHrP(1-34) can hinge at Arg19/Arg20

Biochem Biophys Res Commun. 1996 Mar 18;220(2):431-6. doi: 10.1006/bbrc.1996.0390.


The structure of the biologically-active mutant of human parathyroid hormone related protein (residues 1-34) containing an Ala substituted for a His in position 9 reveals two segments of helix extending from Glu4 to Lys13 and from Phe22 to Ala34, with a reverse turn from Gln16 to Arg19. The C-terminal region contains the bulk of the PTH receptor binding site in an amphipathic helix and is capable of hinging at Arg19/Arg20. The region of the molecule containing full antagonist properties is thus confined to the C-terminal helix.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algorithms
  • Amino Acid Sequence
  • Arginine*
  • Binding Sites
  • Humans
  • Magnetic Resonance Spectroscopy
  • Molecular Sequence Data
  • Parathyroid Hormone-Related Protein*
  • Peptide Fragments / chemistry*
  • Peptide Fragments / metabolism
  • Protein Structure, Secondary
  • Proteins / chemistry*
  • Proteins / metabolism
  • Receptors, Parathyroid Hormone / metabolism*


  • Parathyroid Hormone-Related Protein
  • Peptide Fragments
  • Proteins
  • Receptors, Parathyroid Hormone
  • parathyroid hormone-related protein (1-34)
  • Arginine