PMID- 10551839
OWN - NLM
STAT- MEDLINE
DCOM- 20000103
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 46
DP  - 1999 Nov 12
TI  - The four terminal components of the complement system are C-mannosylated on
      multiple tryptophan residues.
PG  - 32786-94
AB  - C-Mannosylation is a unique form of protein glycosylation, involving the
      C-glycosidic attachment of a mannosyl residue to the indole moiety of Trp. In the
      two examples found so far, human RNase 2 and interleukin-12, only the first Trp
      in the recognition motif WXXW is specifically C-mannosylated. To establish the
      generality of protein C-mannosylation, and to learn more about its mechanism, the
      terminal components of the human complement system (C6, C7, C8,and C9), which
      contain multiple and complex recognition motifs, were examined. Together with C5b
      they form the cytolytic agent, the membrane attack complex. These are the first
      proteins that are C-mannosylated on more than one Trp residue as follows: six in 
      C6, four in C7, C8alpha, and C8beta, and two in C9. Thus, from the 113 Trp
      residues in the complete membrane attack complex, 50 were found to undergo
      C-mannosylation. The other important finding is that in C6, C7, C8, and C9 Trp
      residues without a second Trp (or another aromatic residue) at the +3 position
      can be C-mannosylated. This shows that they must contain an additional
      C-mannosylation signal. Whether this is encoded in the primary or tertiary
      structure is presently unknown. Finally, all modified Trp residues are part of
      the highly conserved core of the thrombospondin type 1 repeats present in these
      proteins. Since this module has been found in a large number of other proteins,
      the results suggest further candidates for C-mannosylation.
FAU - Hofsteenge, J
AU  - Hofsteenge J
AD  - Friedrich Miescher-Institut, Switzerland. hofsteen@fmi.ch
FAU - Blommers, M
AU  - Blommers M
FAU - Hess, D
AU  - Hess D
FAU - Furmanek, A
AU  - Furmanek A
FAU - Miroshnichenko, O
AU  - Miroshnichenko O
LA  - eng
PT  - Journal Article
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (C(2)-mannosyltryptophan)
RN  - 0 (Complement Membrane Attack Complex)
RN  - 0 (Glycopeptides)
RN  - 0 (Glycoproteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Peptide Fragments)
RN  - 0 (Thrombospondins)
RN  - 8DUH1N11BX (Tryptophan)
RN  - PHA4727WTP (Mannose)
SB  - IM
MH  - Complement Membrane Attack Complex/*chemistry
MH  - Glycopeptides/chemistry
MH  - Glycoproteins/chemistry
MH  - Glycosylation
MH  - Humans
MH  - Macromolecular Substances
MH  - Magnetic Resonance Spectroscopy
MH  - Mannose/*chemistry
MH  - Mass Spectrometry
MH  - Peptide Fragments/chemistry
MH  - Thrombospondins/chemistry
MH  - Tryptophan/*analogs & derivatives/chemistry
EDAT- 1999/11/07 00:00
MHDA- 1999/11/07 00:01
CRDT- 1999/11/07 00:00
PHST- 1999/11/07 00:00 [pubmed]
PHST- 1999/11/07 00:01 [medline]
PHST- 1999/11/07 00:00 [entrez]
AID - 10.1074/jbc.274.46.32786 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 12;274(46):32786-94. doi: 10.1074/jbc.274.46.32786.