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- EMDB-50623: carvedilol-B1AR-arrestin2-V2Rpp complex -

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Basic information

Entry
Database: EMDB / ID: EMD-50623
Titlecarvedilol-B1AR-arrestin2-V2Rpp complex
Map data
Sample
  • Complex: carvedilol-B1AR-arrestin2-V2Rpp complex
    • Complex: B1AR
    • Complex: arrestin2
KeywordsG protein-coupled receptor / B1-adrenergic receptor / carvedilol / arrestin2 / biased agonism. / MEMBRANE PROTEIN
Biological speciesHomo sapiens (human) / Meleagris gallopavo (turkey)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.5 Å
AuthorsTatli M / Abiko LA / Petrovic I / Stahlberg H / Grzesiek S
Funding support Switzerland, 4 items
OrganizationGrant numberCountry
Swiss National Science FoundationCRSK-3_195592 Switzerland
Swiss National Science Foundation31-201270 Switzerland
Swiss National Science FoundationIZLIZ3-200298 Switzerland
Swiss National Science Foundation310030_188548 Switzerland
CitationJournal: Proc Natl Acad Sci U S A / Year: 2025
Title: Arrestin recognizes GPCRs independently of the receptor state.
Authors: Ivana Petrovic / Meltem Tatli / Samit Desai / Anne Grahl / Dongchun Ni / Henning Stahlberg / Anne Spang / Stephan Grzesiek / Layara Akemi Abiko /
Abstract: Only two nonvisual arrestins recognize many hundreds of different, intracellularly phosphorylated G protein-coupled receptors (GPCRs). Due to the highly dynamic nature of GPCR•arrestin complexes, ...Only two nonvisual arrestins recognize many hundreds of different, intracellularly phosphorylated G protein-coupled receptors (GPCRs). Due to the highly dynamic nature of GPCR•arrestin complexes, the critical determinants of GPCR-arrestin recognition have remained largely unclear. We show here that arrestin2 recruitment to the β-adrenergic receptor (βAR) can be induced by an arrestin-activating phosphopeptide that is not covalently linked to the receptor and that the recruitment is independent of the presence and type of the orthosteric receptor ligand. Apparently, the arrestin-receptor interaction is driven by the conformational switch within arrestin induced by the phosphopeptide, whereas the electrostatic attraction toward the receptor phosphosites may only play an auxiliary role. Extensive NMR observations show that in contrast to previous static GPCR•arrestin complex structures, the βAR complex with the beta-blocker carvedilol and arrestin2 is in a G protein-inactive conformation. The insensitivity to the specific receptor conformation provides a rationale for arrestin's promiscuous recognition of GPCRs and explains the arrestin-biased agonism of carvedilol, which largely blocks G protein binding, while still enabling arrestin engagement.
History
DepositionJun 11, 2024-
Header (metadata) releaseApr 30, 2025-
Map releaseApr 30, 2025-
UpdateMay 28, 2025-
Current statusMay 28, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50623.png

Downloads & links

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Map

FileDownload / File: emd_50623.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.66 Å/pix.
x 300 pix.
= 197.4 Å		0.66 Å/pix.
x 300 pix.
= 197.4 Å		0.66 Å/pix.
x 300 pix.
= 197.4 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.658 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0989
Minimum - Maximum-0.54470897 - 0.3625359
Average (Standard dev.)0.0038776037 (±0.02239264)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 197.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_50623_msk_1.map
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Additional map: #1

Fileemd_50623_additional_1.map
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Half map: #1

Fileemd_50623_half_map_1.map
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Half map: #2

Fileemd_50623_half_map_2.map
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Sample components

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Entire : carvedilol-B1AR-arrestin2-V2Rpp complex

EntireName: carvedilol-B1AR-arrestin2-V2Rpp complex
Components
  • Complex: carvedilol-B1AR-arrestin2-V2Rpp complex
    • Complex: B1AR
    • Complex: arrestin2

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Supramolecule #1: carvedilol-B1AR-arrestin2-V2Rpp complex

SupramoleculeName: carvedilol-B1AR-arrestin2-V2Rpp complex / type: complex / ID: 1 / Parent: 0
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #2: B1AR

SupramoleculeName: B1AR / type: complex / ID: 2 / Parent: 1
Source (natural)Organism: Meleagris gallopavo (turkey)

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Supramolecule #3: arrestin2

SupramoleculeName: arrestin2 / type: complex / ID: 3 / Parent: 1
Source (natural)Organism: Homo sapiens (human)

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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
Component:
ConcentrationFormulaName
20.0 mMC8H18N2O4SHEPES
100.0 mMNaClNaCl
0.01 %C47H88O22LMNG
10.0 mMC24H26N2O4carvedilol
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec.
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 28.0 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 101282
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
FSC plot (resolution estimation)

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