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- W2029480770 abstract "The amino acid sequences of the human (h) and rat (r) follitropin receptors (FSHR) are ∼89% identical, but the half-time of internalization of agonist mediated by the rFSHR is ∼3 times faster than that of the hFSHR. Chimeras of the hFSHR and the rFSHR showed that this difference in rate is dictated mostly by the serpentine domain. Further analysis identified six residues, two non-contiguous residues in the transmembrane helix 4 (Leu/Thr in the rFSHR and Met/Ile in the hFSHR), three non-contiguous residues in the third intracellular loop (Thr/Thr/Lys in the rFSHR and Ile/Asn/Arg in the hFSHR), and one in transmembrane helix 7 (Tyr in the rFSHR and His in the hFSHR) that are fully responsible for the difference in the rates of internalization of the hFSHR and the rFSHR." @default.
- W2029480770 created "2016-06-24" @default.
- W2029480770 creator A5034096994 @default.
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- W2029480770 date "2000-10-01" @default.
- W2029480770 modified "2023-09-29" @default.
- W2029480770 title "Multiple Distant Amino Acid Residues Present in the Serpentine Region of the Follitropin Receptor Modulate the Rate of Agonist-induced Internalization" @default.
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- W2029480770 doi "https://doi.org/10.1074/jbc.m005528200" @default.
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