Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.

@article{Pereira1998HumanBI,
  title={Human beta-tryptase is a ring-like tetramer with active sites facing a central pore.},
  author={Pedro Jos{\'e} Barbosa Pereira and Andreas Bergner and Sandra Macedo-Ribeiro and Robert Huber and Gabriele Matschiner and Hans Fritz and Christian Sommerhoff and Wolfram Bode},
  journal={Nature},
  year={1998},
  volume={392 6673},
  pages={306-11}
}
Human tryptase, a mast-cell-specific serine proteinase that may be involved in causing asthma and other allergic and inflammatory disorders, is unique in two respects: it is enzymatically active only as a heparin-stabilized tetramer, and it is resistant to all known endogenous proteinase inhibitors. The 3-A crystal structure of human beta-tryptase in a complex with 4-amidinophenyl pyruvic acid shows four quasi-equivalent monomers arranged in a square flat ring of pseudo 222 symmetry. Each… CONTINUE READING

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