Title : Characterization of a posttranslational fucosylation in the growth factor
domain of urinary
plasminogen activator
Abstract :
- A posttranslational modification site in natural and recombinant urinary-type plasminogen activators (urokinases; EC 3.4.21.31) has been localized to Thr-18 , in the growth factor domain of the molecule
- This is the region of urinary plasminogen activator responsible for its specific receptor binding
- An unusual carbohydrate-protein linkage, a single monosaccharide, fucose, covalently attached directly to threonine in the peptide , is described here
- The glycan moiety and the site of modification have been identified with mass spectrometry and confirmed by carbohydrate com position analysis, Edman degradation, and one- and two-dimensional NMR studies
- This type of modification is normally not detected without mass spectrometry because the fucose- threonine bond is hydrolyzed under standard acidic conditions of the amino acid analysis and Edman sequencing
- This modification may be widely found in other proteins
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. fucosylation, , -, the growth factor domain, domain
- 3. attached, , -, An unusual carbohydrate-protein linkage, peptide
- 3. attached, , -, An unusual carbohydrate-protein linkage, threonine
- 3. attached, , -, a single monosaccharide, peptide
- 3. attached, , -, a single monosaccharide, threonine
- 3. attached, , -, fucose, peptide
- 3. attached, , -, fucose, threonine
- 5. fucose-threonine, , -, the fucose-threonine bond, threonine
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):