Probing the conformational and dynamical effects of O-glycosylation within the immunodominant region of a MUC1 peptide tumor antigen.

@article{Schuman2003ProbingTC,
  title={Probing the conformational and dynamical effects of O-glycosylation within the immunodominant region of a MUC1 peptide tumor antigen.},
  author={Jason T. Schuman and Andwayne P. Campbell and R. Rao Koganty and Bryan Michael Longenecker},
  journal={The journal of peptide research : official journal of the American Peptide Society},
  year={2003},
  volume={61 3},
  pages={
          91-108
        }
}
MUC1 mucin is a large transmembrane glycoprotein, the extracellular domain of which is formed by a repeating 20 amino acid sequence, GVTSAPDTRPAPGSTAPPAH. In normal breast epithelial cells, the extracellular domain is densely covered with highly branched complex carbohydrate structures. However, in neoplastic breast tissue, the extracellular domain is under-glycosylated, resulting in the exposure of a highly immunogenic core peptide epitope (PDTRP in bold above), as well as in the exposure of… CONTINUE READING
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