NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata.

@article{Antuch1994NMRSS,
  title={NMR solution structure of the recombinant tick anticoagulant protein (rTAP), a factor Xa inhibitor from the tick Ornithodoros moubata.},
  author={W Antuch and Peter G{\"u}ntert and Martin Urs Billeter and T R Hawthorne and Hugo Grossenbacher and Kurt W{\"u}thrich},
  journal={FEBS letters},
  year={1994},
  volume={352 2},
  pages={251-7}
}
The solution structure of the recombinant tick anticoagulant protein (rTAP) was determined by 1H nuclear magnetic resonance (NMR) spectroscopy in aqueous solution at pH 3.6 and 36 degrees C. rTAP is a 60-residue protein functioning as a highly specific inhibitor of the coagulation protease factor Xa, which was originally isolated from the tick Ornithodoros moubata. Its regular secondary structure consists of a two-stranded antiparallel beta-sheet with residues 22-28 and 32-38, and an alpha… CONTINUE READING

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