Structural features of the C-terminus from the human neurokinin-1 receptor

Mikhail Orel, Esteve Padrós, Joan Manyosa

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

The neurokinin-1 receptor (NK1R) is a G-protein coupled receptor found in the central and peripheral nervous systems of vertebrates, and is responsible for many physiological processes. The C-terminus domain seems to be essential for coupling to the corresponding G-protein and β-arrestin, and is important for receptor desensitization, internalization and recycling. We have focused our study on expression of the human NK1R (hNK1R) C-terminus in Escherichia coli, and its purification and characterization, in order to elucidate its structural properties. CD and Fourier transform infrared spectroscopy showed that the hNK1R C-terminus, rather than having a random structure, has well-defined secondary-structure patterns. The presence of three tyrosine residues in the primary sequence of the hNK1R C-terminus facilitated the use of UV and fluorescence spectroscopy techniques which revealed tyrosine fluorescence and UV absorption at anomalous wavelengths. In their entirety, the results show that the hNK1R C-terminus has clearly defined secondary (25% α-helix, 27% unordered structure and 48% β-sheets and β-turns) and tertiary structures which, it is believed, are tightly related to its multiple functions. © 2012 The Authors Journal compilation © 2012 FEBS.
Original languageEnglish
Pages (from-to)2357-2367
JournalFEBS Journal
Volume279
Issue number13
DOIs
Publication statusPublished - 1 Jul 2012

Keywords

  • CD spectroscopy
  • FTIR spectroscopy
  • G-protein coupled receptors
  • Tyrosine fluorescence
  • UV spectroscopy

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