title: Protein C-mannosylation: facts and questions.
abstract: Among the posttranslational modifications of proteins, glycosylation is probably the most abundant one. Two main types of protein glycosylation have been known for several years, namely N-glycosylation and O-glycosylation. Their biochemical properties, structure and biosynthesis, have been described extensively. Their biological functions are also known for a number of proteins, although in many cases the function remains speculative despite continuous efforts. A few years ago, a new type of protein glycosylation was found, which is different from the above-mentioned ones. It was called C-glycosylation, since the sugar is linked to the protein through a carbon-carbon bond. This article reviews the biochemistry of C-glycosylation, the biosynthetic pathway and structural requirements. Possible biological functions of this modification are also discussed.
authors: Friedrich Miescher-Institut, Basel, Switzerland. ola@fmi.ch
authors: A
authors: A
authors: Furmanek
authors: J
authors: J
authors: Hofsteenge
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D004722:Endoribonucleases / Q000737:chemistry; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000032:analysis*; D011486:Protein C / Q000737:chemistry*; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000032:analysis / Q000737:chemistry
chemical_list: C101500:C(2)-mannosyltryptophan; D011486:Protein C; D014364:Tryptophan; D004722:Endoribonucleases; C029494:ribonuclease U; D008358:Mannose