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

FEBS Letters

Schreier, Shirley⁴  Toma, Flavio³  Carvalho, Regina S.H.²  Paiva, Antonio C.M.²  Pertinhez, Thelma A.⁴  Tabak, Marcel¹  Nakaie, Clóvis R.² 

[1] Instituto de Química de São Carlos, Universidade de São Paulo, São Carlos, Brazil;Departamento de Biofísica, Universidade Federal de São Paulo, São Paulo, Brazil;Départment d'Ingénierie et d'Études des Proteéines, Commissariat à l'Energie Atomique, Saclay, France;Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo, Brazil

关键词: Receptor;    Loop;    Peptide-lipid interaction;    Signal transduction;    Spectroscopic technique;   

DOI  :  10.1016/0014-5793(95)01222-Z

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown