Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF binding.

@article{Buckway2001MutationOT,
  title={Mutation of three critical amino acids of the N-terminal domain of IGF-binding protein-3 essential for high affinity IGF binding.},
  author={Caroline K Buckway and Elizabeth M. Wilson and Maria Ahls{\'e}n and Peter Bang and Y. L. Oh and Ron G. Rosenfeld},
  journal={The Journal of clinical endocrinology and metabolism},
  year={2001},
  volume={86 10},
  pages={4943-50}
}
The N-terminal domain is conserved in all members of the IGF-binding protein superfamily. Most recently, studies have demonstrated the importance of an IGF-binding protein N-terminal hydrophobic pocket for IGF binding. To examine more critically the amino acids important for IGF binding within the full-length IGF-binding protein-3 protein while minimizing changes in the tertiary structure, we targeted residues I56, L80, and L81 within the proposed hydrophobic pocket for mutation. With a single… CONTINUE READING

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