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- EMDB-35136: Follicle stimulating hormone receptor -

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Basic information

Entry
Database: EMDB / ID: EMD-35136
TitleFollicle stimulating hormone receptorFollicle-stimulating hormone receptor
Map data
Sample
  • Complex: Follicle stimulating hormone receptorFollicle-stimulating hormone receptor
    • Protein or peptide: Follicle-stimulating hormone receptor
Function / homology
Function and homology information


follicle-stimulating hormone receptor activity / Hormone ligand-binding receptors / follicle-stimulating hormone signaling pathway / female gamete generation / gonad development / cellular response to follicle-stimulating hormone stimulus / regulation of protein kinase A signaling / G protein-coupled peptide receptor activity / female gonad development / hormone-mediated signaling pathway ...follicle-stimulating hormone receptor activity / Hormone ligand-binding receptors / follicle-stimulating hormone signaling pathway / female gamete generation / gonad development / cellular response to follicle-stimulating hormone stimulus / regulation of protein kinase A signaling / G protein-coupled peptide receptor activity / female gonad development / hormone-mediated signaling pathway / adenylate cyclase-activating G protein-coupled receptor signaling pathway / male gonad development / G alpha (s) signalling events / spermatogenesis / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of ERK1 and ERK2 cascade / receptor complex / G protein-coupled receptor signaling pathway / membrane / plasma membrane
Similarity search - Function
Follicle stimulating hormone receptor / Gonadotropin hormone receptor, transmembrane domain / Gonadotropin hormone receptor transmembrane region / Glycoprotein hormone receptor family / BspA type Leucine rich repeat region / BspA type Leucine rich repeat region (6 copies) / Leucine rich repeat N-terminal domain / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / Leucine-rich repeat domain superfamily ...Follicle stimulating hormone receptor / Gonadotropin hormone receptor, transmembrane domain / Gonadotropin hormone receptor transmembrane region / Glycoprotein hormone receptor family / BspA type Leucine rich repeat region / BspA type Leucine rich repeat region (6 copies) / Leucine rich repeat N-terminal domain / Leucine-rich repeat N-terminal domain / Leucine rich repeat N-terminal domain / 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
Follicle-stimulating hormone receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.0 Å
AuthorsDuan J / Xu P / Yang J / Ji Y / Zhang H / Mao C / Luan X / Jiang Y / Zhang Y / Zhang S / Xu HE
Funding support China, 1 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32130022 China
CitationJournal: Nat Commun / Year: 2023
Title: Mechanism of hormone and allosteric agonist mediated activation of follicle stimulating hormone receptor.
Authors: Jia Duan / Peiyu Xu / Huibing Zhang / Xiaodong Luan / Jiaqi Yang / Xinheng He / Chunyou Mao / Dan-Dan Shen / Yujie Ji / Xi Cheng / Hualiang Jiang / Yi Jiang / Shuyang Zhang / Yan Zhang / H Eric Xu /
Abstract: Follicle stimulating hormone (FSH) is an essential glycoprotein hormone for human reproduction, which functions are mediated by a G protein-coupled receptor, FSHR. Aberrant FSH-FSHR signaling causes ...Follicle stimulating hormone (FSH) is an essential glycoprotein hormone for human reproduction, which functions are mediated by a G protein-coupled receptor, FSHR. Aberrant FSH-FSHR signaling causes infertility and ovarian hyperstimulation syndrome. Here we report cryo-EM structures of FSHR in both inactive and active states, with the active structure bound to FSH and an allosteric agonist compound 21 f. The structures of FSHR are similar to other glycoprotein hormone receptors, highlighting a conserved activation mechanism of hormone-induced receptor activation. Compound 21 f formed extensive interactions with the TMD to directly activate FSHR. Importantly, the unique residue H615 in FSHR plays an essential role in determining FSHR selectivity for various allosteric agonists. Together, our structures provide a molecular basis of FSH and small allosteric agonist-mediated FSHR activation, which could inspire the design of FSHR-targeted drugs for the treatment of infertility and controlled ovarian stimulation for in vitro fertilization.
History
DepositionJan 14, 2023-
Header (metadata) releaseMar 22, 2023-
Map releaseMar 22, 2023-
UpdateMar 22, 2023-
Current statusMar 22, 2023Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_35136.png

Downloads & links

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Map

FileDownload / File: emd_35136.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.045 Å
Density
Contour LevelBy AUTHOR: 0.01
Minimum - Maximum-0.012874393 - 0.03900403
Average (Standard dev.)0.00025958096 (±0.0026796414)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 208.99998 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_35136_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_35136_half_map_2.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : Follicle stimulating hormone receptor

EntireName: Follicle stimulating hormone receptorFollicle-stimulating hormone receptor
Components
  • Complex: Follicle stimulating hormone receptorFollicle-stimulating hormone receptor
    • Protein or peptide: Follicle-stimulating hormone receptor

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Supramolecule #1: Follicle stimulating hormone receptor

SupramoleculeName: Follicle stimulating hormone receptor / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Follicle-stimulating hormone receptor

MacromoleculeName: Follicle-stimulating hormone receptor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 76.97193 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: LGSGCHHRIC HCSNRVFLCQ ESKVTEIPSD LPRNAIELRF VLTKLRVIQK GAFSGFGDLE KIEISQNDVL EVIEADVFSN LPKLHEIRI EKANNLLYIN PEAFQNLPNL QYLLISNTGI KHLPDVHKIH SLQKVLLDIQ DNINIHTIER NSFVGLSFES V ILWLNKNG ...String:
LGSGCHHRIC HCSNRVFLCQ ESKVTEIPSD LPRNAIELRF VLTKLRVIQK GAFSGFGDLE KIEISQNDVL EVIEADVFSN LPKLHEIRI EKANNLLYIN PEAFQNLPNL QYLLISNTGI KHLPDVHKIH SLQKVLLDIQ DNINIHTIER NSFVGLSFES V ILWLNKNG IQEIHNCAFN GTQLDELNLS DNNNLEELPN DVFHGASGPV ILDISRTRIH SLPSYGLENL KKLRARSTYN LK KLPTLEK LVALMEASLT YPSHCCAFAN WRRQISELHP ICNKSILRQE VDYMTQARGQ RSSLAEDNES SYSRGFDMTY TEF DYDLCN EVVDVTCSPK PDAFNPCEDI MGYNILRVLI WFISILAITG NIIVLVILTT SQYKLTVPRF LMCNLAFADL CIGI YLLLI ASVDIHTKSQ YHNYAIDWQT GAGCDAAGFF TVFASELSVY TLTAITLERW HTITHAMQLD CKVQLRHAAS VMVMG WIFA FAAALFPIFG ISSYMKVSIC LPMDIDSPLS QLYVMSLLVL NVLAFVVICG CYIHIYLTVR NPNIVSSSSD TRIAKR MAM LIFTDFLCMA PISFFAISAS LKVPLITVSK AKILLVLFHP INSCANPFLY AIFTKNFRRD FFILLSKCGC YEMQAQI YR TETSSTVHNT HPRNGHCSSA PRVTNGSTYI LVPLSHLAQN

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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: 7.5
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: OTHER / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.2 µm
Image recordingFilm or detector model: FEI FALCON IV (4k 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: 6.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 356211

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