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- EMDB-74081: NTSR1-Gi-NTS(8-13), GTP-bound Complex in the Canonical, AHD Open ... -

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Basic information

Entry
Database: EMDB / ID: EMD-74081
TitleNTSR1-Gi-NTS(8-13), GTP-bound Complex in the Canonical, AHD Open State (C-Open-GTP), MSP1D1
Map data
Sample
  • Complex: NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State
KeywordsComplex / Agonist / SIGNALING PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsRobertson MJ
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)R00 HD107581 United States
Cancer Prevention and Research Institute of Texas (CPRIT)RR230042 United States
CitationJournal: Nature / Year: 2026
Title: Snapshots of the dynamic basis of NTSR1 G protein subtype promiscuity.
Authors: Alina A Vo / Arnab Modak / Sumin Lu / Scott C Blanchard / Nevin A Lambert / Michael J Robertson /
Abstract: G-protein-coupled receptors (GPCRs) are capable of signalling through four families of G protein α subunits. Although hundreds of nucleotide-free GPCR-G protein complex structures have been solved, ...G-protein-coupled receptors (GPCRs) are capable of signalling through four families of G protein α subunits. Although hundreds of nucleotide-free GPCR-G protein complex structures have been solved, the mechanism of G protein subtype selectivity remains poorly understood, with recent studies suggesting a role for dynamic nucleotide-bound intermediate states. Here we use time-resolved cryo-electron microscopy to visualize the GTP-induced activation of Gαβγ and Gαβγ heterotrimers bound to the neurotensin receptor 1 (NTSR1), which has been demonstrated to be highly promiscuous in G protein coupling and to possess unusual conformations in the nucleotide-free complex. We resolve ensembles of states along the G protein activation pathway, with differences in the structures and their relative populations between Gα and Gα. Structural analysis reveals a key role for several motifs, including intracellular loop 2 (ICL2) and ICL3, in stabilizing the observed intermediate states. Our results are supported by molecular dynamics simulations and kinetic bioluminescence resonance energy transfer experiments, which reveal that the stability of these intermediate states and the signalling of various G proteins are correlated with ICL2 and ICL3 sequences. Single-molecule fluorescence assays of GTP-induced NTSR1-G protein complex dissociation reveal that NTSR1 is liberated significantly faster from Gα, consistent with the relative lack of stable Gα-GTP intermediate states compared with Gα. These findings highlight that transient intermediate-state complexes along the G protein activation pathway have an important role in G protein selection that cannot be explained by nucleotide-free states alone.
History
DepositionNov 26, 2025-
Header (metadata) releaseMar 25, 2026-
Map releaseMar 25, 2026-
UpdateMar 25, 2026-
Current statusMar 25, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_74081.png

Downloads & links

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Map

FileDownload / File: emd_74081.map.gz / Format: CCP4 / Size: 83.7 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.)
0.95 Å/pix.
x 280 pix.
= 266. Å		0.95 Å/pix.
x 280 pix.
= 266. Å		0.95 Å/pix.
x 280 pix.
= 266. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.95 Å
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Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.281
Minimum - Maximum-1.895503 - 2.7955651
Average (Standard dev.)-0.000076805234 (±0.037450004)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 266.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #1

Fileemd_74081_half_map_1.map
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Half map: #2

Fileemd_74081_half_map_2.map
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Sample components

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Entire : NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State

EntireName: NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State
Components
  • Complex: NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State

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Supramolecule #1: NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State

SupramoleculeName: NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State
type: complex / ID: 1 / Parent: 0
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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 55.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.4000000000000001 µm / Nominal defocus min: 0.6 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: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 305309
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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