Positions of disulfide bonds and N-glycosylation site in juvenile hormone binding protein

The juvenile hormone binding protein (JHBP) from Galleria mellonella hemolymph is a glycoprotein composed of 225 amino acid residues. It contains four Cys residues forming two disulfide bridges. In this study, the topography of the disulfide bonds as well as the site of glycan attachment in the JHBP...

Full description

Saved in:
Bibliographic Details
Published in:Archives of biochemistry and biophysics 2004-01, Vol.421 (2), p.260-266
Main Authors: Dębski, Janusz, Wysłouch-Cieszyńska, Aleksandra, Dadlez, Michał, Grzelak, Krystyna, Kłudkiewicz, Barbara, Kołodziejczyk, Robert, Lalik, Anna, Ożyhar, Andrzej, Kochman, Marian
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - blood
Carrier Proteins - chemistry
Carrier Proteins - metabolism
Cystine - metabolism
Disulfide bridges
Galleria mellonella hemolymph
Glycosylation
Glycosylation site
Insect Proteins
JHBP
Juvenile hormone binding protein
Larva - chemistry
Larva - metabolism
Lepidoptera - chemistry
Lepidoptera - metabolism
Protein Isoforms
Protein Structure, Tertiary
Sequence Analysis, Protein
Spectrometry, Mass, Electrospray Ionization
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The juvenile hormone binding protein (JHBP) from Galleria mellonella hemolymph is a glycoprotein composed of 225 amino acid residues. It contains four Cys residues forming two disulfide bridges. In this study, the topography of the disulfide bonds as well as the site of glycan attachment in the JHBP molecule from G. mellonella was determined, using electrospray mass spectrometry. The MS analysis was performed on tryptic digests of JHBP. Our results show that the disulfide bridges link Cys 10 and Cys 17, and Cys 151 and Cys 195. Of the two potential N-glycosylation sites in JHBP, Asn 4, and Asn 94, only Asn 94 is glycosylated. This site of glycosylation is also found in the fully biologically active recombinant JHBP expressed in the yeast Pichia pastoris.
ISSN:0003-9861
1096-0384
DOI:10.1016/j.abb.2003.10.019