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J. Biol. Chem., Vol. 266, Issue 22, 14251-14255, 08, 1991
DK Reed, RJ Ryan and DJ McCormick
Synthetic peptides were used to probe the structure-function relationships
between human choriotropin (hCG) and the lutropin (LH) receptor.
Previously, a peptide region of the alpha subunit of hCG, residues 26-46,
had been shown to inhibit binding of 125I-hCG to the LH receptor in rat
ovarian membranes (Charlesworth, M.C., McCormick, D.J., Madden, B., and
Ryan, R.J. (1987) J. Biol. Chem. 262, 13409-13416). To determine which
residues are important for this inhibitory activity, peptides were
truncated from either the amino or carboxyl terminus, or individual
residues were substituted with alanine. The amino-terminal boundary was
determined to be Gly-30 and the carboxyl-terminal boundary, Lys-44. This
core peptide contained all the residues needed for full activity of the
parent peptide 26-46. Arg-35 and Phe-33 were particularly important
residues; when they were substituted with alanine, the peptide inhibitory
potencies were decreased. Ser-43, Arg- 42, Cys-32, and Cys-31 were also
important but to a lesser degree. These results are consistent with
predictions based on chemical and enzymatic modification studies and
provide insight into which residues are important for interaction between
hCG and the LH receptor.
Residues in the alpha subunit of human choriotropin that are important for interaction with the lutropin receptor
Department of Biochemistry and Molecular Biology, Mayo Foundation, Rochester, Minnesota 55905.
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