Conformational changes upon binding of a receptor loop to lipid structures: possible role in signal transduction

Thelma A. Pertinhez, Clóvis R. Nakaie, Regina S H Carvalho, Antonio C M Paiva, Marcel Tabak, Flavio Toma, Shirley Schreier

Research output: Contribution to journalArticlepeer-review

Abstract

The mas oncogene codes for a seven transmembrane helix protein. The amino acid sequence 253-266, from the third extracellular loop and beginning of helix 7, was synthesized either blocked or carrying an amino acid spin label at the N-terminus. Peptide binding to bilayers and micelles was monitored by ESR, fluorescence and circular dichroism. Binding induced tighter lipid packing, and caused an increase of peptide secondary structure. While binding to bilayers occurred only when peptide and phospholipid bore opposite charges, in micelles the interaction took place irrespective of charge. The results suggest that changes in lipid packing could modulate conformational changes in receptor loops related to the triggering of signal transduction.

Original languageEnglish
Pages (from-to)239-242
Number of pages4
JournalFEBS Letters
Volume375
Issue number3
DOIs
Publication statusPublished - Nov 20 1995

Keywords

  • Loop
  • Peptide-lipid interaction
  • Receptor
  • Signal transduction
  • Spectroscopic technique

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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