Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.

@article{Wyss1995CompositionAS,
  title={Composition and sequence specific resonance assignments of the heterogeneous N-linked glycan in the 13.6 kDa adhesion domain of human CD2 as determined by NMR on the intact glycoprotein.},
  author={Daniel F. Wyss and Joon Sig Choi and Gerhard Wagner},
  journal={Biochemistry},
  year={1995},
  volume={34 5},
  pages={1622-34}
}
CD2, a T cell specific surface adhesion receptor, is critically important for T lymphocytes to mediate their regulatory and effector functions. The amino terminal domain of human CD2 is responsible for cell adhesion, binding to CD58 on antigen-presenting cells or target cells. This adhesion domain in human CD2 contains a single high-mannose N-glycan. This carbohydrate or part of it appears to be required to maintain the native conformation of the polypeptide and its ability to bind CD58. To… CONTINUE READING

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