Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling.

@article{Jiang2000IdentificationOS,
  title={Identification of substrate orienting and phosphorylation sites within tryptophan hydroxylase using homology-based molecular modeling.},
  author={George C-T Jiang and George J. Yohrling and Jeffrey D. Schmitt and Kent E. Vrana},
  journal={Journal of molecular biology},
  year={2000},
  volume={302 4},
  pages={1005-17}
}
Tryptophan hydroxylase (TPH) is the initial and rate-limiting enzyme in the biosynthesis of serotonin. The inherent instability of TPH has prevented a crystallographic structure from being resolved. For this reason, multiple sequence alignment-based molecular modeling was utilized to generate a full-length model of human TPH. Previously determined crystal coordinates of two highly homologous proteins, phenylalanine hydroxylase and tyrosine hydroxylase, were used as templates. Analysis of the… CONTINUE READING
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