Characterization of a region of the lutropin receptor extracellular domain near transmembrane helix 1 that is important in ligand-mediated signaling.

作者: Carlos A. Alvarez , Prema Narayan , Jianing Huang , David Puett

DOI: 10.1210/ENDO.140.4.6624

关键词:

摘要: The lutropin receptor (LHR), a member of the G protein-coupled family, contains relatively large N-terminal extracellular domain, accounting for about half and responsible high affinity ligand binding, standard heptahelical portion with connecting loops C-terminal tail. LHR other two glycoprotein hormone receptors, i.e. follitropin TSH contain an invariant 10-amino acid residue sequence, FNPCEDIMGY (residues 328–337 in rat LHR), domain separated by only few amino residues from beginning transmembrane helix 1. In view nature this region three receptors preliminary data literature on importance Glu332 Asp333 signal transduction, we undertook systematic investigation all 10 because may function as switch or trigger communicating binding to conformationa...

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