[English] 日本語
Yorodumi
- EMDB-64618: Composite map of the G protein-coupled receptor 1 (GPR1) bound to... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-64618
TitleComposite map of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2
Map dataCryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2
Sample
  • Complex: G protein-coupled receptor 1 in complex with chemerin and beta-arrestin2
    • Protein or peptide: Retinoic acid receptor responder protein 2
    • Protein or peptide: Nanobody 32
    • Protein or peptide: Single-chain fragment variable 30 (scFv30)
    • Protein or peptide: Beta-arrestin-2,Beta-arrestin-1
    • Protein or peptide: Chemerin-like receptor 2,Vasopressin V2 receptor
  • Ligand: CHOLESTEROL HEMISUCCINATE
KeywordsG protein-coupled receptor 1 / chemerin / beta-arrestin 2 / signaling protein / MEMBRANE PROTEIN/IMMUNE SYSTEM / MEMBRANE PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


postsynaptic signal transduction / positive regulation of synaptic transmission, dopaminergic / adipokinetic hormone binding / adipokinetic hormone receptor activity / renal water retention / Defective AVP does not bind AVPR2 and causes neurohypophyseal diabetes insipidus (NDI) / platelet dense granule lumen / Vasopressin-like receptors / regulation of systemic arterial blood pressure by vasopressin / vasopressin receptor activity ...postsynaptic signal transduction / positive regulation of synaptic transmission, dopaminergic / adipokinetic hormone binding / adipokinetic hormone receptor activity / renal water retention / Defective AVP does not bind AVPR2 and causes neurohypophyseal diabetes insipidus (NDI) / platelet dense granule lumen / Vasopressin-like receptors / regulation of systemic arterial blood pressure by vasopressin / vasopressin receptor activity / positive regulation of cardiac muscle cell differentiation / protein kinase B binding / WNT5A-dependent internalization of FZD4 / regulation of lipid catabolic process / antifungal innate immune response / angiotensin receptor binding / hemostasis / TGFBR3 regulates TGF-beta signaling / desensitization of G protein-coupled receptor signaling pathway / negative regulation of toll-like receptor signaling pathway / Activation of SMO / telencephalon development / embryonic digestive tract development / antifungal humoral response / response to caloric restriction / negative regulation of interleukin-8 production / negative regulation of interleukin-12 production / positive regulation of chemotaxis / G protein-coupled receptor internalization / arrestin family protein binding / negative regulation of natural killer cell mediated cytotoxicity / neuropeptide binding / adult walking behavior / G protein-coupled dopamine receptor signaling pathway / negative regulation of interleukin-1 beta production / Lysosome Vesicle Biogenesis / negative regulation of NF-kappaB transcription factor activity / positive regulation of cardiac muscle hypertrophy / stress fiber assembly / Golgi Associated Vesicle Biogenesis / positive regulation of macrophage chemotaxis / positive regulation of vasoconstriction / positive regulation of Rho protein signal transduction / pseudopodium / positive regulation of systemic arterial blood pressure / negative regulation of interleukin-6 production / positive regulation of intracellular signal transduction / positive regulation of receptor internalization / negative regulation of tumor necrosis factor production / endocytic vesicle / negative regulation of Notch signaling pathway / enzyme inhibitor activity / neuropeptide signaling pathway / D1 dopamine receptor binding / positive regulation of fat cell differentiation / retinoid metabolic process / activation of adenylate cyclase activity / cellular response to hormone stimulus / insulin-like growth factor receptor binding / clathrin-coated pit / response to cytokine / negative regulation of protein ubiquitination / negative regulation of canonical NF-kappaB signal transduction / extracellular matrix / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / transforming growth factor beta receptor signaling pathway / GTPase activator activity / cytoplasmic vesicle membrane / Activated NOTCH1 Transmits Signal to the Nucleus / response to activity / cell chemotaxis / excitatory postsynaptic potential / clathrin-coated endocytic vesicle membrane / Signaling by high-kinase activity BRAF mutants / G protein-coupled receptor binding / G protein-coupled receptor activity / MAP2K and MAPK activation / receptor internalization / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / positive regulation of protein phosphorylation / chemotaxis / Signaling by RAF1 mutants / Signaling by moderate kinase activity BRAF mutants / Paradoxical activation of RAF signaling by kinase inactive BRAF / Signaling downstream of RAS mutants / endocytic vesicle membrane / Vasopressin regulates renal water homeostasis via Aquaporins / Signaling by BRAF and RAF1 fusions / insulin receptor signaling pathway / Platelet degranulation / Cargo recognition for clathrin-mediated endocytosis / glucose homeostasis / protein transport / Clathrin-mediated endocytosis / : / Thrombin signalling through proteinase activated receptors (PARs) / cytoplasmic vesicle / ubiquitin-dependent protein catabolic process / defense response to Gram-negative bacterium / G alpha (s) signalling events
Similarity search - Function
Chemerin-like receptor 2 / Retinoic acid receptor responder protein 2 / Vasopressin V2 receptor / Vasopressin receptor / Formyl peptide receptor-related / Arrestin, conserved site / Arrestins signature. / Arrestin / Arrestin, N-terminal / Arrestin-like, N-terminal ...Chemerin-like receptor 2 / Retinoic acid receptor responder protein 2 / Vasopressin V2 receptor / Vasopressin receptor / Formyl peptide receptor-related / Arrestin, conserved site / Arrestins signature. / Arrestin / Arrestin, N-terminal / Arrestin-like, N-terminal / Arrestin C-terminal-like domain / Arrestin (or S-antigen), N-terminal domain / Arrestin (or S-antigen), C-terminal domain / Arrestin (or S-antigen), C-terminal domain / Arrestin-like, C-terminal / Cystatin 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) / Immunoglobulin E-set
Similarity search - Domain/homology
Vasopressin V2 receptor / Beta-arrestin-2 / Chemerin-like receptor 2 / Beta-arrestin-1 / Retinoic acid receptor responder protein 2
Similarity search - Component
Biological speciesHomo sapiens (human) / Escherichia phage EcSzw-2 (virus)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsCai H / Lin X / Zhao L / He M / Yu J / Zhang B / Ma Y / Xie C / Shui W / Zhao Q ...Cai H / Lin X / Zhao L / He M / Yu J / Zhang B / Ma Y / Xie C / Shui W / Zhao Q / Zhu Y / Wu B
Funding support China, 2 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)82121005 China
National Natural Science Foundation of China (NSFC)32401012 China
CitationJournal: Science / Year: 2025
Title: Noncanonical agonist-dependent and -independent arrestin recruitment of GPR1
Authors: Cai H / Lin X / Zhao L / He M / Yu J / Zhang B / Ma Y / Chang X / Tang Y / Luo T / Jiang J / Ma M / Song W / Ma L / Chu X / Yi C / Chen K / Han S / Xie C / Shui W / Zhao Q / Zhu Y / Wu B
History
DepositionMay 15, 2025-
Header (metadata) releaseNov 19, 2025-
Map releaseNov 19, 2025-
UpdateNov 19, 2025-
Current statusNov 19, 2025Processing site: PDBc / Status: Released

-
Structure visualization

Supplemental images

emd_64618.png

Downloads & links

-
Map

FileDownload / File: emd_64618.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 256 pix.
= 274.176 Å		1.07 Å/pix.
x 256 pix.
= 274.176 Å		1.07 Å/pix.
x 256 pix.
= 274.176 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.071 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.19
Minimum - Maximum-1.1090516 - 2.396503
Average (Standard dev.)0.0091756005 (±0.043335244)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 274.176 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Sample components

-
Entire : G protein-coupled receptor 1 in complex with chemerin and beta-ar...

EntireName: G protein-coupled receptor 1 in complex with chemerin and beta-arrestin2
Components
  • Complex: G protein-coupled receptor 1 in complex with chemerin and beta-arrestin2
    • Protein or peptide: Retinoic acid receptor responder protein 2
    • Protein or peptide: Nanobody 32
    • Protein or peptide: Single-chain fragment variable 30 (scFv30)
    • Protein or peptide: Beta-arrestin-2,Beta-arrestin-1
    • Protein or peptide: Chemerin-like receptor 2,Vasopressin V2 receptor
  • Ligand: CHOLESTEROL HEMISUCCINATE

-
Supramolecule #1: G protein-coupled receptor 1 in complex with chemerin and beta-ar...

SupramoleculeName: G protein-coupled receptor 1 in complex with chemerin and beta-arrestin2
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)

-
Macromolecule #1: Retinoic acid receptor responder protein 2

MacromoleculeName: Retinoic acid receptor responder protein 2 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.720475 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MKTIIALSYI FCLVFAELTE AQRRGLQVAL EEFHKHPPVQ WAFQETSVES AVDTPFPAGI FVRLEFKLQQ TSCRKRDWKK PECKVRPNG RKRKCLACIK LGSEDKVLGR LVHCPIETQV LREAEEHQET QCLRVQRAGE DPHSFYFPGQ FAFS

UniProtKB: Retinoic acid receptor responder protein 2

-
Macromolecule #2: Nanobody 32

MacromoleculeName: Nanobody 32 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Escherichia phage EcSzw-2 (virus)
Molecular weightTheoretical: 13.238716 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString:
QVQLQESGGG LVQAGGSLRL SCVVSGFFFD TVTMAWYRRA PGKHRELVAS ATAGGTTTYA DSVKDRFTIS RDNAKNTVYL QMNSLKPED TAVYYCNTFV RSLSWGQGTQ VTVSSHHHHH H

-
Macromolecule #3: Single-chain fragment variable 30 (scFv30)

MacromoleculeName: Single-chain fragment variable 30 (scFv30) / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 26.157861 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQYKYVPVTF GQGTKVEIKG TTAASGSSGG SSSGAEVQLV ESGGGLVQPG GSLRLSCAAS GFNVYSSSIH W VRQAPGKG ...String:
SDIQMTQSPS SLSASVGDRV TITCRASQSV SSAVAWYQQK PGKAPKLLIY SASSLYSGVP SRFSGSRSGT DFTLTISSLQ PEDFATYYC QQYKYVPVTF GQGTKVEIKG TTAASGSSGG SSSGAEVQLV ESGGGLVQPG GSLRLSCAAS GFNVYSSSIH W VRQAPGKG LEWVASISSY YGYTYYADSV KGRFTISADT SKNTAYLQMN SLRAEDTAVY YCARSRQFWY SGLDYWGQGT LV TVSSA

-
Macromolecule #4: Beta-arrestin-2,Beta-arrestin-1

MacromoleculeName: Beta-arrestin-2,Beta-arrestin-1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.50848 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MGEKPGTRVF KKSSPNGKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK DRKVFVTLTV AFRYGREDLD VLGLSFRKDL FIATYQAFP PVPNPPRPPT RLQDRLLRKL GQHAHPFFFT IPQNLPSSVT LQPGPEDTGK ALGVDFEIRA FVAKSLEEKS H KRNSVRLV ...String:
MGEKPGTRVF KKSSPNGKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK DRKVFVTLTV AFRYGREDLD VLGLSFRKDL FIATYQAFP PVPNPPRPPT RLQDRLLRKL GQHAHPFFFT IPQNLPSSVT LQPGPEDTGK ALGVDFEIRA FVAKSLEEKS H KRNSVRLV IRKVQFAPEK PGPQPSAETT RHFLMSDRSL HLEASLDKEL YYHGEPLNVN VHVTNNSTKT VKKIKVSVRQ YA DIVLFST AQYKVPVAQL EQDDQVSPSS TFSKVYTITP LLSDNREKRG LALDGKLKHE DTNLASSTIV KEGANKEVLG ILV SYRVKV KLVVSRGGDV SVELPFVLMH PKPKEEPPHR EVPENETPVD TNL

UniProtKB: Beta-arrestin-2, Beta-arrestin-1

-
Macromolecule #5: Chemerin-like receptor 2,Vasopressin V2 receptor

MacromoleculeName: Chemerin-like receptor 2,Vasopressin V2 receptor / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.03184 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MKTIIALSYI FCLVFAGSWS HPQFEKGSGA GASAGSWSHP QFEKGSDYKD DDDKEFLEVL FQGPEDLEET LFEEFENYSY DLDYYSLES DLEEKVQLGV VHWVSLVLYC LAFVLGIPGN AIVIWFTGFK WKKTVTTLWF LNLAIADFIF LLFLPLYISY V AMNFHWPF ...String:
MKTIIALSYI FCLVFAGSWS HPQFEKGSGA GASAGSWSHP QFEKGSDYKD DDDKEFLEVL FQGPEDLEET LFEEFENYSY DLDYYSLES DLEEKVQLGV VHWVSLVLYC LAFVLGIPGN AIVIWFTGFK WKKTVTTLWF LNLAIADFIF LLFLPLYISY V AMNFHWPF GIWLCKANSF TAQLNMFASV FFLTVISLDH YIHLIHPVLS HRHRTLKNSL IVIIFIWLLA SLIGGPALYF RD TVEFNNH TLCYNNFQKH DPDLTLIRHH VLTWVKFIIG YLFPLLTMSI CYLCLIFKVK KRSILISSRH FWTILVVVVA FVV CWTPYH LFSIWELTIH HNSYSHHVMQ AGIPLSTGLA FLNSCLNPIL YVLISKKFQA RFRSSVAEIA RGRTPPSLGP QDE (SEP)C(TPO)(TPO)A(SEP) (SEP)(SEP)LAKDTSS

UniProtKB: Chemerin-like receptor 2, Vasopressin V2 receptor

-
Macromolecule #6: CHOLESTEROL HEMISUCCINATE

MacromoleculeName: CHOLESTEROL HEMISUCCINATE / type: ligand / ID: 6 / Number of copies: 1 / Formula: Y01
Molecular weightTheoretical: 486.726 Da
Chemical component information

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 2.1875 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: NONE
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 123307
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more