Assignment of the ligand binding site of the porcine estradiol receptor to the N-terminal 17 kDa part of domain E.
Ligand-filled porcine estradiol receptor was adsorbed to heparin-Sepharose, from which a 26 kDa fragment was released by papain. Its mass was reduced to a 17 kDa fragment by trypsin. The sedimentation velocities of both estradiol binding fragments increased after reaction with the MAB 13H2. The same antibody identified the denatured fragments on Western blots. The N-terminal 21 amino acid sequence was obtained from the 17 kDa peptide which corresponds to amino acids 303-323 of the human receptor with four amino acids exchanged. This indicates that the ligand binding site resides in the N-terminal 17 kDa portion of domain E.
Thole
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Max-Planck-Institut für experimentelle Endokrinologie, Hannover, Germany.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D004958:Estradiol / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011959:Receptors, Estradiol / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D013552:Swine; D014357:Trypsin
D010446:Peptide Fragments; D011959:Receptors, Estradiol; D004958:Estradiol; D014357:Trypsin