A region in the human glycoprotein hormone alpha-subunit important in holoprotein formation and receptor binding.
Using site-directed mutagenesis of the human glycoprotein hormone alpha-subunit, we have shown that single replacements of Ala36 and Pro38 with Glu and Asp, respectively, result in mutant subunits that do not bind significantly to hCG beta. In contrast, the replacement of Lys44 with Ala did not interfere with hCG beta binding, but the resulting holoprotein failed to exhibit high affinity binding to the LH/CG receptor. These results in conjunction with other data suggest that the region of human alpha between positions 33-45 contains several amino acid residues that participate in subunit binding and others that function in receptor binding.
Xia
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Department of Biochemistry, University of Georgia, Athens 30602.
Chen
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Puett
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D000595:Amino Acid Sequence; D001667:Binding, Competitive; D006063:Chorionic Gonadotropin / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D015292:Glycoprotein Hormones, alpha Subunit / Q000235:genetics* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D015345:Oligonucleotide Probes / Q000235:genetics; D011974:Receptors, LH / Q000378:metabolism*
D006063:Chorionic Gonadotropin; D015292:Glycoprotein Hormones, alpha Subunit; D015345:Oligonucleotide Probes; D011974:Receptors, LH