Secondary structure and topology of the transmembrane domain of Syndecan-2 in detergent micelles

FEBS Letters

article

Qingxin Li¹  Hui Qi Ng²  CongBao Kang² 

[1] Institute of Chemical and Engineering Sciences, Agency for Science, Technology and Research (A*STAR);Experimental Therapeutics Centre, Experimental Drug Development Centre (EDDC), Agency for Science, Technology and Research (A*STAR)

关键词: membrane topology;    NMR;    syndecan;    transmembrane domain;    type-I membrane proteins;   

DOI  :  10.1002/1873-3468.13335

来源: John Wiley & Sons Ltd.

【 摘 要 】

Syndecans are single-span membrane proteins playing important roles in cell– cell and cell–matrix interactions. The transmembrane domain of syndecans is critical for signal transduction across the cell membrane. Here, the structure of the transmembrane domain of syndecan-2 in detergent micelles was investigated using solution NMR spectroscopy. Backbone resonance assignment was obtained, and NMR studies show that the transmembrane domain forms a helix in detergent micelles, which is also supported by the hydrogen and deuterium exchange experiment. A study of the dynamics revealed the rigid structure of the transmembrane domain formed in solution, and paramagnetic relaxation enhancement defined the topology of the transmembrane domain in detergent micelles. This structural analysis may facilitate a better understanding of the role of the syndecan-2 transmembrane domain in signal transduction.

【 授权许可】

Unknown