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- EMDB-31599: luteinizing hormone/choriogonadotropin receptor -

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Basic information

Entry
Database: EMDB / ID: EMD-31599
Titleluteinizing hormone/choriogonadotropin receptor
Map data
Sample
  • Complex: luteinizing hormone/choriogonadotropin receptor
    • Protein or peptide: Lutropin-choriogonadotropic hormone receptor
Function / homology
Function and homology information


luteinizing hormone receptor activity / choriogonadotropin hormone receptor activity / choriogonadotropin hormone binding / regulation of steroid hormone biosynthetic process / development of secondary male sexual characteristics / luteinizing hormone signaling pathway / positive regulation of inositol trisphosphate biosynthetic process / Hormone ligand-binding receptors / ovulation cycle process / cellular response to gonadotropin stimulus ...luteinizing hormone receptor activity / choriogonadotropin hormone receptor activity / choriogonadotropin hormone binding / regulation of steroid hormone biosynthetic process / development of secondary male sexual characteristics / luteinizing hormone signaling pathway / positive regulation of inositol trisphosphate biosynthetic process / Hormone ligand-binding receptors / ovulation cycle process / cellular response to gonadotropin stimulus / positive regulation of hormone biosynthetic process / cellular response to luteinizing hormone stimulus / protein targeting to lysosome / male genitalia development / G protein-coupled peptide receptor activity / arachidonic acid secretion / positive regulation of calcium ion transport into cytosol / seminiferous tubule development / uterus development / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / peptide hormone binding / centriolar satellite / positive regulation of calcium-mediated signaling / ovarian follicle development / activation of adenylate cyclase activity / hormone-mediated signaling pathway / positive regulation of release of sequestered calcium ion into cytosol / adenylate cyclase-activating G protein-coupled receptor signaling pathway / cognition / male gonad development / phospholipase C-activating G protein-coupled receptor signaling pathway / ATPase binding / G alpha (s) signalling events / spermatogenesis / receptor complex / endosome / response to xenobiotic stimulus / G protein-coupled receptor signaling pathway / extracellular space / identical protein binding / plasma membrane
Similarity search - Function
Lutropin-choriogonadotropic hormone receptor / Glycoprotein hormone receptor family / BspA type Leucine rich repeat region / BspA type Leucine rich repeat region (6 copies) / Leucine-rich repeat domain superfamily / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family)
Similarity search - Domain/homology
Lutropin-choriogonadotropic hormone receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsDuan J / Xu P / Cheng X / Mao C / Croll T / He X / Shi J / Luan X / Yin W / You E ...Duan J / Xu P / Cheng X / Mao C / Croll T / He X / Shi J / Luan X / Yin W / You E / Liu Q / Zhang S / Jiang H / Zhang Y / Jiang Y / Xu HE
Funding support China, 1 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2018YFA0507002 China
CitationJournal: Nature / Year: 2021
Title: Structures of full-length glycoprotein hormone receptor signalling complexes.
Authors: Jia 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 / ...Authors: Jia 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 /
Abstract: Luteinizing 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.
History
DepositionJul 31, 2021-
Header (metadata) releaseSep 29, 2021-
Map releaseSep 29, 2021-
UpdateFeb 16, 2022-
Current statusFeb 16, 2022Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.115
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.115
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7fij
  • Surface level: 0.115
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_31599.png

Downloads & links

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Map

FileDownload / File: emd_31599.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.045 Å
Density
Contour LevelBy AUTHOR: 0.115 / Movie #1: 0.115
Minimum - Maximum-0.061703984 - 3.3685334
Average (Standard dev.)0.0011517144 (±0.020771433)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions192192192
Spacing192192192
CellA=B=C: 200.63998 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0451.0451.045
M x/y/z192192192
origin x/y/z0.0000.0000.000
length x/y/z200.640200.640200.640
α/β/γ90.00090.00090.000
start NX/NY/NZ-220-220-220
NX/NY/NZ440440440
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS192192192
D min/max/mean-0.0623.3690.001

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Supplemental data

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Sample components

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Entire : luteinizing hormone/choriogonadotropin receptor

EntireName: luteinizing hormone/choriogonadotropin receptor
Components
  • Complex: luteinizing hormone/choriogonadotropin receptor
    • Protein or peptide: Lutropin-choriogonadotropic hormone receptor

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Supramolecule #1: luteinizing hormone/choriogonadotropin receptor

SupramoleculeName: luteinizing hormone/choriogonadotropin receptor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Macromolecule #1: Lutropin-choriogonadotropic hormone receptor

MacromoleculeName: Lutropin-choriogonadotropic hormone receptor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 78.629797 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: DYKDDDDVEN LYFQGASALC PEPCNCVPDG ALRCPGPTAG LTRLSLAYLP VKVIPSQAFR GLNEVIKIEI SQIDSLERIE ANAFDNLLN LSEILIQNTK NLRYIEPGAF INLPRLKYLS ICNTGIRKFP DVTKVFSSES NFILEICDNL HITTIPGNAF Q GMNNESVT ...String:
DYKDDDDVEN LYFQGASALC PEPCNCVPDG ALRCPGPTAG LTRLSLAYLP VKVIPSQAFR GLNEVIKIEI SQIDSLERIE ANAFDNLLN LSEILIQNTK NLRYIEPGAF INLPRLKYLS ICNTGIRKFP DVTKVFSSES NFILEICDNL HITTIPGNAF Q GMNNESVT LKLYGNGFEE VQSHAFNGTT LTSLELKENV HLEKMHNGAF RGATGPKTLD ISSTKLQALP SYGLESIQRL IA TSSYSLK KLPSRETFVN LLEATLTYPS HCCAFRNLPT KEQNFSHSIS ENFSKQCEST VRKVNNKTLY SSMLAESELS GWD YEYGFC LPKTPRCAPE PDAFNPCEDI MGYDFLRVLI WLINILAIMG NMTVLFVLLT SRYKLTVPRF LMCNLSFADF CMGL YLLLI ASVDSQTKGQ YYNHAIDWQT GSGCSTAGFF TVFASELSVY TLTVITLERW HTITYAIHLD QKLRLRHAIL IMLGG WLFS SLIAMLPLVG VSNYMKVSIC FPMDVETTLS QVYILTILIL NVVAFFIICA CYIKIYFAVR NPELMATNKD TKIAKK MAI LIFTDFTCMA PISFFAISAA FKVPLITVTN SKVLLVLFYP INSCANPFLY AIFTKTFQRD FFLLLSKFGC CKRRAEL YR RKDFSAYTSN CKNGFTGSNK PSQSTLKLST LHCQGTALLD KTRYTECHHH HHHHH

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 70.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 311538

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