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  • proteins
  • Its substrate specificity suggests that Tsp may contain a substrate recognition domain, which selectively binds to the nonpolar C-termini of substrate proteins, separate from its catalytic site. (embl.de)
  • ADP ribosylation factors (ARFs), which are members of the Ras superfamily of GTP-binding proteins, are critical components of vesicular trafficking pathways in eukaryotes. (embl-heidelberg.de)
  • Like Ras, ARFs are active in their GTP-bound form, and their duration of activity is controlled by GTPase-activating proteins (GAPs), which assist ARFs in hydrolyzing GTP to GDP. (embl-heidelberg.de)
  • structure
  • Differences between the structure of the resting enzyme and the structure of the NO-LOX complex that may be observed with EPR include both the positions of the electron orbitals and the spatial orientation of the nitric oxide-iron bond, from which one may be able to infer the positions and coordination of the other iron ligands. (fsu.edu)
  • domain
  • Systematic deletion mutagenesis of Tsp localized the binding site to amino acids 206-307, a region that completely encompasses the putative PDZ domain (217-301). (embl.de)
  • Site-directed mutagenesis of a surface residue at the peptide binding site of the PDZ domain, valine 229, to Glu or Gln resulted in an increase in the K(M) value but had no effect on the k(cat) value. (embl.de)
  • surface
  • Peptide binding of the ligand takes place in an elongated surface groove as an anti-parallel beta-strand interacts with the beta-B strand and the B helix. (embl.de)