Secondary structure of the promastigote surface protease of Leishmania

FEBS Letters

Etges, Robert¹  Jähnig, Fritz¹ 

[1] Max-Planck-Institut für Biologie, Corrensstr. 38, D-7400 Tübingen, FRG

关键词: Raman spectroscopy;    Membrane-bound protein;    Metalloproteinase;   

DOI  :  10.1016/0014-5793(88)81035-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

By Raman spectroscopic analysis we have determined the secondary structure of the promastigote surface protease, named PSP or gp63, of Leishmania major. It consist of nearly 50% antiparallel β-strand, and less than 20% α-helix. These results are contrasted with the predominantly α-helical VSGs of the African trypanosomes and the α-helical metalloprotease thermolysin. The PSP of Leishmania thus represents a novel kind of membrane-anchored protease.

【 授权许可】

Unknown