skip to main content
Language:
Search Limited to: Search Limited to: Resource type Show Results with: Show Results with: Search type Index

O-Linked fucose and other post-translational modifications unique to EGF modules

Glycobiology (Oxford), 1993-06, Vol.3 (3), p.219-224 [Peer Reviewed Journal]

ISSN: 0959-6658 ;EISSN: 1460-2423 ;DOI: 10.1093/glycob/3.3.219 ;PMID: 8358148

Full text available

Citations Cited by
  • Title:
    O-Linked fucose and other post-translational modifications unique to EGF modules
  • Author: Harris, Reed J. ; Spellman, Michael W.
  • Subjects: Amino Acid Sequence ; Animals ; Blood Coagulation Factors - biosynthesis ; Carbohydrate Sequence ; Conserved Sequence ; Epidermal Growth Factor - biosynthesis ; fucose ; Fucose - metabolism ; Glycoproteins - biosynthesis ; Glycosylation ; growth factor modules ; Humans ; Molecular Sequence Data ; post-translational modifications ; Protein Processing, Post-Translational ; Sequence Homology, Amino Acid ; xylose
  • Is Part Of: Glycobiology (Oxford), 1993-06, Vol.3 (3), p.219-224
  • Description: Three types of unusual post-translational modification have been found within conserved amino acid sequences in epidermal growth factor homology regions (EGF modules) of some multidomain proteins. β-Hydroxyaspartate and β-hydroxyasparagine are found within -Cys-Xxx-Asp/Asn-Xxx-Xxx-Xxx-Xxx-Tyr/Phe-Xxx-Cys-Xxx-Cys- sequences. (Xylα1→3)Xylα1→3Glcβ1→O-Ser glycans at conserved sites within -Cys-Xxx-Ser-Xxx-Pro-Cys- sequences have been reported in several proteins. Fucα1→O-Thr/Ser Modifications have been found at conserved sites within -Cys-Xxx-Xxx-Gly-Gly-Thr/Ser-Cys- sequences. More recently, it has been discovered that the Ser residue corresponding to the potential O-fucosylation site in human factor IX carries the novel tetrasaccharide NeuAcα2→6Galβ1→4GlcNAcβ1→3Fucα1→O-Ser; this tetrasaccharide can be considered to be an extension of the Fucα1→O moiety. The consensus sequences for these post-translational modifications are in close proximity to each other; e.g. human factor IX has all three unusual modifications within a 12 amino acid linear sequence. In proteins with multiple EGF modules, the O-glycosidic modifications have been found only within the N-terminal EGF module; β-hydroxyaspartate/asparagine residues are not restricted in the same fashion. Little is known yet about the functions of, or possible relationships between, any of these modifications.
  • Publisher: England: Oxford University Press
  • Language: English
  • Identifier: ISSN: 0959-6658
    EISSN: 1460-2423
    DOI: 10.1093/glycob/3.3.219
    PMID: 8358148
  • Source: MEDLINE
    Alma/SFX Local Collection
Back to results list
INSPIRE LIBRARY - TON DUC THANG UNIVERSITY (84-028) 37 755 057 Feedback
19 Nguyen Huu Tho St. Dist.7, HCM thuvien@tdtu.edu.vn

Copyright © 2017 INSPIRE LIBRARY - TON DUC THANG UNIVERSITY

Searching Remote Databases, Please Wait