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Identification of Binding Sites with Differing Affinity and Potency for Relaxin Analogues on LGR7 and LGR8 Receptors
Author(s) -
HALLS MICHELLE L.,
BATHGATE ROSS A.,
SUDO SATOKO,
KUMAGAI JIN,
BOND COURTNEY P.,
SUMMERS ROGER J.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1282.004
Subject(s) - ectodomain , receptor , relaxin , biology , chemistry , potency , binding site , biochemistry , microbiology and biotechnology , in vitro
A bstract : This study defines the pharmacologic characteristics of LGR7 and LGR8, the receptors for H2 relaxin and INSL3 respectively, and determines the relative activity of relaxin‐related peptides. We show, for the first time, the availability of two binding sites at LGR8 and confirm the presence of two sites at LGR7. Relaxin‐related peptides had differing rank orders of affinity and potency at LGR7 and LGR8, but chimeric receptors were highly similar to their ectodomain‐origin native receptors. The high‐affinity site on the ectodomain coupled efficiently to cAMP production, whereas the low‐affinity site in the transmembrane region coupled with decreased efficiency.