Identification of residues essential for progesterone binding to uteroglobin by site-directed mutagenesis

@article{Peter1991IdentificationOR,
  title={Identification of residues essential for progesterone binding to uteroglobin by site-directed mutagenesis},
  author={W. Peter and H. Br{\"u}ller and G. Vriend and M. Beato and G. Suske},
  journal={The Journal of Steroid Biochemistry and Molecular Biology},
  year={1991},
  volume={38},
  pages={27-33}
}
In order to identify amino acids directly involved in progesterone binding to rabbit uteroglobin we have mutated Phe 6, Tyr 21 and Thr 60 by site-directed mutagenesis of the uteroglobin cDNA. These residues have been postulated previously to participate in progesterone binding. High-level expression of the mutated uteroglobin cDNAs in Escherichia coli yields recombinant protein mutants that, like natural uteroglobin, form stable dimers, suggesting that the tertiary structure of the protein has… Expand
Full-Length Complementary DNA and the Derived Amino Acid Sequence of Horse Uteroglobin1
The Uteroglobin Fold
The Crystal Structure of the Major Cat Allergen Fel d 1, a Member of the Secretoglobin Family*
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References

SHOWING 1-10 OF 22 REFERENCES
Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 A resolution.
Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34 A resolution.
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