PMID- 10066782
OWN - NLM
STAT- MEDLINE
DCOM- 19990413
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 11
DP  - 1999 Mar 12
TI  - Disulfide bond structure and N-glycosylation sites of the extracellular domain of
      the human interleukin-6 receptor.
PG  - 7207-15
AB  - The high affinity interleukin-6 (IL-6) receptor is a hexameric complex consisting
      of two molecules each of IL-6, IL-6 receptor (IL-6R), and the high affinity
      converter and signaling molecule, gp130. The extracellular "soluble" part of the 
      IL-6R (sIL-6R) consists of three domains: an amino-terminal Ig-like domain and
      two fibronectin-type III (FN III) domains. The two FN III domains comprise the
      cytokine-binding domain defined by a set of 4 conserved cysteine residues and a
      WSXWS sequence motif. Here, we have determined the disulfide structure of the
      human sIL-6R by peptide mapping in the absence and presence of reducing agent.
      Mass spectrometric analysis of these peptides revealed four disulfide bonds and
      two free cysteines. The disulfides Cys102-Cys113 and Cys146-Cys157 are consistent
      with known cytokine-binding domain motifs, and Cys28-Cys77 with known Ig
      superfamily domains. An unusual cysteine connectivity between Cys6-Cys174, which 
      links the Ig-like and NH2-terminal FN III domains causing them to fold back onto 
      each other, has not previously been observed among cytokine receptors. The two
      free cysteines (Cys192 and Cys258) were detected as cysteinyl-cysteines, although
      a small proportion of Cys258 was reactive with the alkylating agent
      4-vinylpyridine. Of the four potential N-glycosylation sites, carbohydrate
      moieties were identified on Asn36, Asn74, and Asn202, but not on Asn226.
FAU - Cole, A R
AU  - Cole AR
AD  - Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research
      (Melbourne Tumour Biology Branch) and The Walter and Eliza Hall Institute of
      Medical Research, Parkville, Victoria 3050, Australia.
FAU - Hall, N E
AU  - Hall NE
FAU - Treutlein, H R
AU  - Treutlein HR
FAU - Eddes, J S
AU  - Eddes JS
FAU - Reid, G E
AU  - Reid GE
FAU - Moritz, R L
AU  - Moritz RL
FAU - Simpson, R J
AU  - Simpson RJ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Antigens, CD)
RN  - 0 (Disulfides)
RN  - 0 (IL6ST protein, human)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Receptors, Interleukin-6)
RN  - 0 (Recombinant Proteins)
RN  - 133483-10-0 (Cytokine Receptor gp130)
RN  - EC 3.4.21.4 (Trypsin)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antigens, CD/metabolism
MH  - CHO Cells
MH  - Cricetinae
MH  - Cytokine Receptor gp130
MH  - Disulfides/chemistry/*metabolism
MH  - Glycosylation
MH  - Humans
MH  - Membrane Glycoproteins/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Molecular Structure
MH  - Peptide Mapping
MH  - Receptors, Interleukin-6/chemistry/*metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Homology, Amino Acid
MH  - Signal Transduction
MH  - Trypsin/metabolism
EDAT- 1999/03/06 00:00
MHDA- 1999/03/06 00:01
CRDT- 1999/03/06 00:00
PHST- 1999/03/06 00:00 [pubmed]
PHST- 1999/03/06 00:01 [medline]
PHST- 1999/03/06 00:00 [entrez]
AID - 10.1074/jbc.274.11.7207 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Mar 12;274(11):7207-15. doi: 10.1074/jbc.274.11.7207.