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Conformational changes upon binding of a receptor loop to lipid structures: possible role in signal transduction
Author(s) -
Pertinhez Thelma A.,
Nakaie Clóvis R.,
Carvalho Regina S.H.,
Paiva Antonio C.M.,
Tabak Marcel,
Toma Flavio,
Schreier Shirley
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01222-z
Subject(s) - circular dichroism , biophysics , conformational change , transmembrane protein , helix (gastropod) , micelle , chemistry , peptide , transmembrane domain , lipid bilayer , signal transduction , phospholipid , peptide sequence , protein secondary structure , amino acid , biochemistry , receptor , membrane , biology , ecology , snail , aqueous solution , gene
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.