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Structure paper

TitleStructures of full-length glycoprotein hormone receptor signalling complexes.
Journal, issue, pagesNature, Vol. 598, Issue 7882, Page 688-692, Year 2021
Publish dateSep 22, 2021
AuthorsJia Duan / Peiyu Xu / Xi Cheng / Chunyou Mao / Tristan Croll / Xinheng He / Jingjing Shi / Xiaodong Luan / Wanchao Yin / Erli You / Qiufeng Liu / Shuyang Zhang / Hualiang Jiang / Yan Zhang / Yi Jiang / H Eric Xu /
PubMed AbstractLuteinizing hormone and chorionic gonadotropin are glycoprotein hormones that are related to follicle-stimulating hormone and thyroid-stimulating hormone. Luteinizing hormone and chorionic ...Luteinizing hormone and chorionic gonadotropin are glycoprotein hormones that are related to follicle-stimulating hormone and thyroid-stimulating hormone. Luteinizing hormone and chorionic gonadotropin are essential to human reproduction and are important therapeutic drugs. They activate the same G-protein-coupled receptor, luteinizing hormone-choriogonadotropin receptor (LHCGR), by binding to the large extracellular domain. Here we report four cryo-electron microscopy structures of LHCGR: two structures of the wild-type receptor in the inactive and active states; and two structures of the constitutively active mutated receptor. The active structures are bound to chorionic gonadotropin and the stimulatory G protein (G), and one of the structures also contains Org43553, an allosteric agonist. The structures reveal a distinct 'push-and-pull' mechanism of receptor activation, in which the extracellular domain is pushed by the bound hormone and pulled by the extended hinge loop next to the transmembrane domain. A highly conserved 10-residue fragment (P10) from the hinge C-terminal loop at the interface between the extracellular domain and the transmembrane domain functions as a tethered agonist to induce conformational changes in the transmembrane domain and G-protein coupling. Org43553 binds to a pocket of the transmembrane domain and interacts directly with P10, which further stabilizes the active conformation. Together, these structures provide a common model for understanding the signalling of glycoprotein hormone receptors and a basis for drug discovery for endocrine diseases.
External linksNature / PubMed:34552239
MethodsEM (single particle)
Resolution3.2 - 4.3 Å
Structure data

31596

7fig

EMDB-31596, PDB-7fig:
luteinizing hormone/choriogonadotropin receptor(S277I)-chorionic gonadotropin-Gs complex
Method: EM (single particle) / Resolution: 3.9 Å

31597

7fih

EMDB-31597, PDB-7fih:
luteinizing hormone/choriogonadotropin receptor(S277I)-chorionic gonadotropin-Gs-Org43553 complex
Method: EM (single particle) / Resolution: 3.2 Å

31598

7fii

EMDB-31598, PDB-7fii:
luteinizing hormone/choriogonadotropin receptor-chorionic gonadotropin-Gs complex
Method: EM (single particle) / Resolution: 4.3 Å

31599

7fij

EMDB-31599, PDB-7fij:
luteinizing hormone/choriogonadotropin receptor
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-55Z:
5-azanyl-N-tert-butyl-2-methylsulfanyl-4-[3-(2-morpholin-4-ylethanoylamino)phenyl]thieno[2,3-d]pyrimidine-6-carboxamide

Source
  • homo sapiens (human)
  • bos taurus (cattle)
  • lama glama (llama)
  • rattus norvegicus (Norway rat)
KeywordsMEMBRANE PROTEIN / glycoprotein hormone receptor / luteinizing hormone / chorionic gonadotropin / GPCR / Gs-protein / choriogonadotropin receptor

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