NMR structure of a minimum activity domain of human parathyroid peptide hormone: Structural origin of receptor activation

J. Jung, W. Lee, S. K. Lim, Y. Kim

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Parathyroid hormone (PTH) which increases osteoblast numbers and bone formation by activating bone-lining cells to osteoblasts plays an important role in calcium and phosphate homeostasis and bone remodeling by activating PTH receptors. To determine the structural origin of a minimum activity domain of hPTH, we initiated a detailed structural determination of the hPTHH14 in aqueous solution using NMR spectroscopy. Circular dichroism and NMR data demonstrated that hPTHH14 maintains a typical helical conformation in both membrane-mimicking environments and 30% TFE solution. The solution structure clearly showed that the residues from Ser3 to Leu11 of hPTHH14 formed a stable helical structure, especially having charged side-chains oriented in opposite directions relative to one another for optimum interaction with the receptor molecule.

Original languageEnglish
Pages (from-to)239-246
Number of pages8
JournalJournal of Peptide Research
Volume60
Issue number5
DOIs
Publication statusPublished - 2002 Nov 1

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology

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