Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.

@article{Moritz2001DeterminationOT,
  title={Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130.},
  author={Robert L. Moritz and Nathan E. Hall and Lisa M. C. Connolly and Richard J. Simpson},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 11},
  pages={
          8244-53
        }
}
gp130 is the common signal transducing receptor subunit for the interleukin-6-type family of cytokines. Its extracellular region (sgp130) is predicted to consist of five fibronectin type III-like domains and an NH2-terminal Ig-like domain. Domains 2 and 3 constitute the cytokine-binding region defined by a set of four conserved cysteines and a WSXWS motif, respectively. Here we determine the disulfide structure of human sgp130 by peptide mapping, in the absence and presence of reducing agent… CONTINUE READING

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