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Yorodumi- PDB-8jps: Structure of Duffy Antigen Receptor for Chemokines (DARC)/ACKR1 i... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8jps | |||||||||||||||
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Title | Structure of Duffy Antigen Receptor for Chemokines (DARC)/ACKR1 in complex with the chemokine, CCL7 (Composite map) | |||||||||||||||
Components |
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Keywords | IMMUNE SYSTEM / GPCR / SIGNALING PROTEIN | |||||||||||||||
Function / homology | Function and homology information regulation of chemokine production / CCR2 chemokine receptor binding / CCR1 chemokine receptor binding / positive regulation of natural killer cell chemotaxis / CCR chemokine receptor binding / lymphocyte chemotaxis / C-C chemokine binding / eosinophil chemotaxis / cellular response to ethanol / chemokine-mediated signaling pathway ...regulation of chemokine production / CCR2 chemokine receptor binding / CCR1 chemokine receptor binding / positive regulation of natural killer cell chemotaxis / CCR chemokine receptor binding / lymphocyte chemotaxis / C-C chemokine binding / eosinophil chemotaxis / cellular response to ethanol / chemokine-mediated signaling pathway / Chemokine receptors bind chemokines / chemokine activity / monocyte chemotaxis / cellular response to interleukin-1 / cytoskeleton organization / Peptide ligand-binding receptors / neutrophil chemotaxis / G protein-coupled receptor activity / response to gamma radiation / recycling endosome / defense response / cellular response to type II interferon / intracellular calcium ion homeostasis / transmembrane signaling receptor activity / chemotaxis / cell-cell signaling / cellular response to tumor necrosis factor / signaling receptor activity / heparin binding / regulation of cell shape / early endosome / positive regulation of ERK1 and ERK2 cascade / positive regulation of cell migration / inflammatory response / G protein-coupled receptor signaling pathway / signal transduction / extracellular space / extracellular region / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.65 Å | |||||||||||||||
Authors | Banerjee, R. / Khanppnavar, B. / Maharana, J. / Saha, S. / Korkhov, V.M. / Shukla, A.K. | |||||||||||||||
Funding support | India, United Kingdom, 4items
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Citation | Journal: Cell(Cambridge,Mass.) / Year: 2024 Title: Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor Authors: Saha, S. / Khanppnavar, B. / Maharana, J. / Kim, H. / Carino, C.M.C. / Daly, C. / Houston, S. / Sharma, S. / Zaidi, N. / Dalal, A. / Mishra, S. / Ganguly, M. / Tiwari, D. / Kumari, P. / ...Authors: Saha, S. / Khanppnavar, B. / Maharana, J. / Kim, H. / Carino, C.M.C. / Daly, C. / Houston, S. / Sharma, S. / Zaidi, N. / Dalal, A. / Mishra, S. / Ganguly, M. / Tiwari, D. / Kumari, P. / Jhingan, G.D. / Yadav, P.N. / Plouffe, B. / Inoue, A. / Chung, K.Y. / Banerjee, R. / Korkhov, V.M. / Shukla, A.K. | |||||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8jps.cif.gz | 114.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8jps.ent.gz | 86.4 KB | Display | PDB format |
PDBx/mmJSON format | 8jps.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8jps_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 8jps_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 8jps_validation.xml.gz | 34.7 KB | Display | |
Data in CIF | 8jps_validation.cif.gz | 49.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jp/8jps ftp://data.pdbj.org/pub/pdb/validation_reports/jp/8jps | HTTPS FTP |
-Related structure data
Related structure data | 36488MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 28073.523 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACKR1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q16570 #2: Protein | Mass: 7594.902 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CCL7, MCP3, SCYA6, SCYA7 / Production host: Escherichia coli (E. coli) / References: UniProt: P80098 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component |
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Molecular weight | Experimental value: NO | ||||||||||||||||||||||||
Source (natural) | Organism: Homo sapiens (human) | ||||||||||||||||||||||||
Source (recombinant) |
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Buffer solution | pH: 7.4 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
-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: 2000 nm / Nominal defocus min: 1000 nm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 58 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||
Particle selection | Num. of particles selected: 25479169 | ||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.65 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 308174 / Symmetry type: POINT | ||||||||||||||||||||||||
Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL | ||||||||||||||||||||||||
Atomic model building | Source name: AlphaFold / Type: in silico model | ||||||||||||||||||||||||
Refine LS restraints |
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