title: Secondary structure of the promastigote surface protease of Leishmania.
abstract: 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 beta-strand, and less than 20% alpha-helix. These results are contrasted with the predominantly alpha-helical VSGs of the African trypanosomes and the alpha-helical metalloprotease thermolysin. The PSP of Leishmania thus represents a novel kind of membrane-anchored protease.
authors.affiliation: Max-Planck-Institut für Biologie, Tübingen, FRG.
authors.forename: F
authors.initials: F
authors.lastname: Jähnig
authors.forename: R
authors.initials: R
authors.lastname: Etges
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D007895:Leishmania tropica / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011487:Protein Conformation
chemical_list: D010447:Peptide Hydrolases