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Open data
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Basic information
| Entry | Database: PDB / ID: 8zjg | |||||||||||||||||||||||||||||||||
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| Title | Cryo-EM structure of human CMKLR1-Gi complex bound to chemerin | |||||||||||||||||||||||||||||||||
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Keywords | MEMBRANE PROTEIN / Chemerin Receptor | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationadipokinetic hormone binding / adipokinetic hormone receptor activity / platelet dense granule lumen / complement receptor activity / regulation of lipid catabolic process / antifungal innate immune response / chemokine receptor activity / embryonic digestive tract development / antifungal humoral response / response to caloric restriction ...adipokinetic hormone binding / adipokinetic hormone receptor activity / platelet dense granule lumen / complement receptor activity / regulation of lipid catabolic process / antifungal innate immune response / chemokine receptor activity / embryonic digestive tract development / antifungal humoral response / response to caloric restriction / negative regulation of interleukin-12 production / positive regulation of chemotaxis / complement receptor mediated signaling pathway / Class A/1 (Rhodopsin-like receptors) / negative regulation of NF-kappaB transcription factor activity / positive regulation of macrophage chemotaxis / positive regulation of systemic arterial blood pressure / positive regulation of fat cell differentiation / retinoid metabolic process / adenylate cyclase inhibitor activity / positive regulation of protein localization to cell cortex / T cell migration / Adenylate cyclase inhibitory pathway / D2 dopamine receptor binding / response to prostaglandin E / regulation of calcium-mediated signaling / adenylate cyclase regulator activity / G protein-coupled serotonin receptor binding / adenylate cyclase-inhibiting serotonin receptor signaling pathway / extracellular matrix / cellular response to forskolin / regulation of mitotic spindle organization / response to activity / skeletal system development / Regulation of insulin secretion / positive regulation of cholesterol biosynthetic process / negative regulation of insulin secretion / G protein-coupled receptor binding / G protein-coupled receptor activity / response to peptide hormone / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / adenylate cyclase-modulating G protein-coupled receptor signaling pathway / centriolar satellite / G-protein beta/gamma-subunit complex binding / Olfactory Signaling Pathway / Activation of the phototransduction cascade / positive regulation of protein phosphorylation / G beta:gamma signalling through PLC beta / Presynaptic function of Kainate receptors / Thromboxane signalling through TP receptor / G protein-coupled acetylcholine receptor signaling pathway / Activation of G protein gated Potassium channels / Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits / G-protein activation / chemotaxis / Prostacyclin signalling through prostacyclin receptor / G beta:gamma signalling through CDC42 / Glucagon signaling in metabolic regulation / G beta:gamma signalling through BTK / Synthesis, secretion, and inactivation of Glucagon-like Peptide-1 (GLP-1) / ADP signalling through P2Y purinoceptor 12 / photoreceptor disc membrane / Sensory perception of sweet, bitter, and umami (glutamate) taste / Glucagon-type ligand receptors / Adrenaline,noradrenaline inhibits insulin secretion / Vasopressin regulates renal water homeostasis via Aquaporins / GDP binding / Glucagon-like Peptide-1 (GLP1) regulates insulin secretion / G alpha (z) signalling events / cellular response to catecholamine stimulus / ADORA2B mediated anti-inflammatory cytokines production / ADP signalling through P2Y purinoceptor 1 / G beta:gamma signalling through PI3Kgamma / insulin receptor signaling pathway / adenylate cyclase-activating dopamine receptor signaling pathway / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / Platelet degranulation / GPER1 signaling / Inactivation, recovery and regulation of the phototransduction cascade / cellular response to prostaglandin E stimulus / G-protein beta-subunit binding / heterotrimeric G-protein complex / G alpha (12/13) signalling events / sensory perception of taste / signaling receptor activity / extracellular vesicle / signaling receptor complex adaptor activity / : / Thrombin signalling through proteinase activated receptors (PARs) / positive regulation of cold-induced thermogenesis / retina development in camera-type eye / G protein activity / positive regulation of cytosolic calcium ion concentration / GTPase binding / Ca2+ pathway / fibroblast proliferation / midbody / High laminar flow shear stress activates signaling by PIEZO1 and PECAM1:CDH5:KDR in endothelial cells / cell cortex / G alpha (i) signalling events Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human)![]() | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.18 Å | |||||||||||||||||||||||||||||||||
Authors | Liu, A.J. / Liu, Y.Z. / Ye, R.D. | |||||||||||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: Commun Biol / Year: 2024Title: Structural basis for full-length chemerin recognition and signaling through chemerin receptor 1. Authors: Aijun Liu / Yezhou Liu / Junlin Wang / Richard D Ye / ![]() Abstract: Chemerin, a chemotactic adipokine, plays essential roles in adipogenesis and inflammation. Serum chemerin concentration is closely associated with obesity and metabolism disorders. The mature form of ...Chemerin, a chemotactic adipokine, plays essential roles in adipogenesis and inflammation. Serum chemerin concentration is closely associated with obesity and metabolism disorders. The mature form of chemerin (residues 21-157) acts primarily through chemerin receptor 1 (CMKLR1) for transmembrane signaling. As a result, CMKLR1 serves as a promising target for therapeutic intervention of immunometabolic diseases such as diabetes and multiple sclerosis. Here, we present a high-resolution cryo-EM structure of CMKLR1-Gi signaling complex bound to biologically active full-length chemerin. The mature chemerin shows binding features distinct from its C-terminal nonapeptide including interaction with both the extracellular loops (ECLs) and the N-terminus of CMKLR1. Combining results from functional assays, our studies demonstrate that chemerin interacts with CMKLR1 in a "two-site" mode similar to chemokine-chemokine receptor interactions, but acting as a "reverse chemokine" by inserting its C-terminus instead of the N-terminus as in the case of chemokines into the transmembrane binding pocket of CMKLR1. These structural insights are expected to help develop synthetic analogs with therapeutic potential. | |||||||||||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8zjg.cif.gz | 266.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8zjg.ent.gz | 209.2 KB | Display | PDB format |
| PDBx/mmJSON format | 8zjg.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8zjg_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 8zjg_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 8zjg_validation.xml.gz | 49.1 KB | Display | |
| Data in CIF | 8zjg_validation.cif.gz | 72.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zj/8zjg ftp://data.pdbj.org/pub/pdb/validation_reports/zj/8zjg | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 60144MC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 2 types, 2 molecules AL
| #1: Protein | Mass: 42362.848 Da / Num. of mol.: 1 / Mutation: M101P Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CMKLR1, CHEMR23, DEZ / Production host: ![]() |
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| #6: Protein | Mass: 15904.175 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RARRES2 / Production host: ![]() |
-Guanine nucleotide-binding protein ... , 3 types, 3 molecules BCG
| #2: Protein | Mass: 37416.930 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNB1 / Production host: ![]() |
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| #3: Protein | Mass: 40153.672 Da / Num. of mol.: 1 / Mutation: G203A, A326S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNAI1 / Production host: ![]() |
| #4: Protein | Mass: 7861.143 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GNG2 / Production host: ![]() |
-Antibody , 1 types, 1 molecules S
| #5: Antibody | Mass: 26337.307 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-Non-polymers , 2 types, 5 molecules 


| #7: Chemical | ChemComp-CLR / #8: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Human chemerin receptor 1-Gi complex bound to chemerin Type: COMPLEX / Entity ID: #1-#6 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.4 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 52 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 3.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 2682313 / Symmetry type: POINT |
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Homo sapiens (human)

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FIELD EMISSION GUN