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 language | English |
|---|---|
| Pages (from-to) | 239-242 |
| Number of pages | 4 |
| Journal | FEBS Letters |
| Volume | 375 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 20 1995 |
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Keywords
- Loop
- Peptide-lipid interaction
- Receptor
- Signal transduction
- Spectroscopic technique
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Cell Biology
- Genetics
- Molecular Biology
- Structural Biology
Cite this
Conformational changes upon binding of a receptor loop to lipid structures : possible role in signal transduction. / Pertinhez, Thelma A.; Nakaie, Clóvis R.; Carvalho, Regina S H; Paiva, Antonio C M; Tabak, Marcel; Toma, Flavio; Schreier, Shirley.
In: FEBS Letters, Vol. 375, No. 3, 20.11.1995, p. 239-242.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Conformational changes upon binding of a receptor loop to lipid structures
T2 - possible role in signal transduction
AU - Pertinhez, Thelma A.
AU - Nakaie, Clóvis R.
AU - Carvalho, Regina S H
AU - Paiva, Antonio C M
AU - Tabak, Marcel
AU - Toma, Flavio
AU - Schreier, Shirley
PY - 1995/11/20
Y1 - 1995/11/20
N2 - 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.
AB - 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.
KW - Loop
KW - Peptide-lipid interaction
KW - Receptor
KW - Signal transduction
KW - Spectroscopic technique
UR - http://www.scopus.com/inward/record.url?scp=0028856941&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028856941&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(95)01222-Z
DO - 10.1016/0014-5793(95)01222-Z
M3 - Article
C2 - 7498508
AN - SCOPUS:0028856941
VL - 375
SP - 239
EP - 242
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -