Journal article
A high-resolution solution structure of a trypanosomatid FYVE domain
HDT Mertens, JM Callaghan, JD Swarbrick, MJ Mcconville, PR Gooley
Protein Science | WILEY | Published : 2007
DOI: 10.1110/ps.073009807
Abstract
FYVE domain proteins play key roles in regulating membrane traffic in eukaryotic cells. The FYVE domain displays a remarkable specificity for the head group of the target lipid, phosphatidylinositol 3-phosphate (PtdIns[3]P). We have identified five putative FYVE domain proteins in the genome of the protozoan parasite Leishmania major, three of which are predicted to contain a functional PtdIns(3)P-binding site. The FYVE domain of one of these proteins, LmFYVE-1, bound PtdIns(3)P in liposome-binding assays and targeted GFP to acidified late endosomes/lysosomes in mammalian cells. The high-resolution solution structure of its N-terminal FYVE domain (LmFYVE-1[1-79]) was solved by nuclear magnet..
View full abstract