Molecular organization of the human serotonin transporter at the air/water interface

FEBS Letters

Baszkin, Adam³  Faivre, Vincent³  Rosilio, Véronique³  Launay, Jean-Marie²  Manivet, Philippe²  Langevin, Dominique¹ 

[1]Laboratoire de Physique des Solides, LPS CNRS, Bâtiment 510, Université Paris-Sud, 91405 Orsay, France

[2]C.R. C. Bernard ‘Pathologie Expérimentale et Communications Cellulaires’, Service de Biochimie, IFR 6, Hôpital Lariboisière AP-HP, 2 rue Ambroise Paré, 75010 Paris, France

[3]Physico-Chimie des Surfaces, UMR CNRS 8612, 5 rue J.B. Clément, 92296 Châtenay-Malabry Cedex, France

关键词: Serotonin;    Transporter;    Surface pressure;    Ellipsometry;    Protein monolayer;    SERT;    serotonin transporter;    5-HT;    5-hydroxytryptophan;   

DOI  :  10.1016/S0014-5793(01)02218-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The serotonin transporter (SERT) is the target of several important antidepressant and psychostimulant drugs. It has been shown that under defined conditions, the transporter spread at the air/water interface was able to bind its specific ligands. In this paper, the interfacial organization of the protein has been assessed from dynamic surface pressure and ellipsometric measurements. For areas comprising between 10 400 and 7100 Ų/molecule, ellipsometric measurements reveal an important change in the thickness of the SERT film. This change was attributed to the reorientation of the transporter molecules from a horizontal to their natural predictive transmembrane orientation. The thickness of the SERT film at 7100 Ų/molecule was found to be approximately equal to 84 Å and coincided well with the theoretical value estimated from the calculations based on the dimensions of α-helices containing membrane proteins. These data suggest that the three-dimensional arrangement of the SERT may be represented as a box with lengths d_z =83–85 Å and d_y or d_x =41–47 Å.

【 授权许可】

Unknown