Progesterone binding to uteroglobin: two alternative orientations of the ligand.

@article{Dunkel1995ProgesteroneBT,
  title={Progesterone binding to uteroglobin: two alternative orientations of the ligand.},
  author={R. Dunkel and G. Vriend and M. Beato and G. Suske},
  journal={Protein engineering},
  year={1995},
  volume={8 1},
  pages={
          71-9
        }
}
Progesterone binding to a homodimer of uteroglobin takes place in a hydrophobic cavity formed by the two subunits. Previous mutational analyses have shown that the tyrosine (21 and 21') and threonine (60 and 60') residues of the uteroglobin dimer are directly involved in progesterone binding. To analyze the contribution of each of the two tyrosines and threonines in the dimer, we have constructed a covalently linked uteroglobin dimer (UGcl) by fusing two uteroglobin cDNAs via a synthetic linker… Expand
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