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TitleStructural basis for activation of the growth hormone-releasing hormone receptor.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5205, Year 2020
Publish dateOct 15, 2020
AuthorsFulai Zhou / Huibing Zhang / Zhaotong Cong / Li-Hua Zhao / Qingtong Zhou / Chunyou Mao / Xi Cheng / Dan-Dan Shen / Xiaoqing Cai / Cheng Ma / Yuzhe Wang / Antao Dai / Yan Zhou / Wen Sun / Fenghui Zhao / Suwen Zhao / Hualiang Jiang / Yi Jiang / Dehua Yang / H Eric Xu / Yan Zhang / Ming-Wei Wang /
PubMed AbstractGrowth hormone-releasing hormone (GHRH) regulates the secretion of growth hormone that virtually controls metabolism and growth of every tissue through its binding to the cognate receptor (GHRHR). ...Growth hormone-releasing hormone (GHRH) regulates the secretion of growth hormone that virtually controls metabolism and growth of every tissue through its binding to the cognate receptor (GHRHR). Malfunction in GHRHR signaling is associated with abnormal growth, making GHRHR an attractive therapeutic target against dwarfism (e.g., isolated growth hormone deficiency, IGHD), gigantism, lipodystrophy and certain cancers. Here, we report the cryo-electron microscopy (cryo-EM) structure of the human GHRHR bound to its endogenous ligand and the stimulatory G protein at 2.6 Å. This high-resolution structure reveals a characteristic hormone recognition pattern of GHRH by GHRHR, where the α-helical GHRH forms an extensive and continuous network of interactions involving all the extracellular loops (ECLs), all the transmembrane (TM) helices except TM4, and the extracellular domain (ECD) of GHRHR, especially the N-terminus of GHRH that engages a broad set of specific interactions with the receptor. Mutagenesis and molecular dynamics (MD) simulations uncover detailed mechanisms by which IGHD-causing mutations lead to the impairment of GHRHR function. Our findings provide insights into the molecular basis of peptide recognition and receptor activation, thereby facilitating the development of structure-based drug discovery and precision medicine.
External linksNat Commun / PubMed:33060564 / PubMed Central
MethodsEM (single particle)
Resolution2.6 Å
Structure data

30505

7cz5

EMDB-30505, PDB-7cz5:
Cryo-EM structure of the human growth hormone-releasing hormone receptor-Gs protein complex
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID

ChemComp-CLR:
CHOLESTEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
  • bos taurus (cattle)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / cognate receptor / Class B G-protein-coupled receptors / single particle

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