Structure of an LGR dimer - an evolutionary predecessor of glycoprotein hormone receptors.

ABSTRACT: The glycoprotein hormones of humans, produced in the pituitary and acting through receptors in the gonads to support reproduction and in the thyroid gland for metabolism, have co-evolved from invertebrate counterparts^1,2. These hormones are heterodimeric cystine-knot proteins; and their receptors bind the cognate hormone at an extracellular domain and transmit the signal of this binding through a transmembrane domain that interacts with a heterotrimeric G protein. Structures determined for the human receptors as isolated for cryogenic electron microscopy (cryo-EM) are all monomeric^3-6 despite compelling evidence for their functioning as dimers^7-10. Here we describe the cryo-EM structure of the homologous receptor from a neuroendocrine pathway that promotes

SUBMITTER: Gong Z 

PROVIDER: S-EPMC11722252 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature