Detection of Zn-binding in domain E of the porcine estradiol receptor.
A 32 kDa fragment of the porcine estradiol receptor, which contains the entire hormone-binding domain E and parts of the adjacent domains D and F, binds 65Zn with high affinity. Nonradioactive Zn and Cu are equally potent competitors, Co and Ni are less effective. The capacity for Zn-binding is pH-dependent, it is abolished by the ethoxycarboxylation of imidazole, but remains unimpaired after the modification of sulfhydryls by vinylpyridine. The presence of a HDXXH motif in domain E of the receptor and the significance of its similarity with the HEXXH zinc-binding motif of metallo-proteases are discussed.
Humeny
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Max-Planck-Institut für Experimentelle Endokrinologie, Hannover, Germany.
Thole
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HH
D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D003300:Copper / Q000378:metabolism; D005260:Female; D006639:Histidine / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008666:Metalloendopeptidases / Q000235:genetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D011959:Receptors, Estradiol / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013552:Swine; D014599:Uterus / Q000737:chemistry / Q000378:metabolism*; D015032:Zinc / Q000378:metabolism*
D010446:Peptide Fragments; D011959:Receptors, Estradiol; D006639:Histidine; D003300:Copper; D008666:Metalloendopeptidases; D015032:Zinc