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- PDB-9l3z: Cryo-EM structure of the inactive chemokine-like receptor 1 (CMKLR1) -
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Open data
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Basic information
Entry | Database: PDB / ID: 9l3z | |||||||||||||||||||||
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Title | Cryo-EM structure of the inactive chemokine-like receptor 1 (CMKLR1) | |||||||||||||||||||||
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![]() | MEMBRANE PROTEIN/IMMUNE SYSTEM / GPCR / CMKLR1 / MEMBRANE PROTEIN-IMMUNE SYSTEM complex | |||||||||||||||||||||
Function / homology | ![]() adipokinetic hormone binding / adipokinetic hormone receptor activity / complement receptor activity / chemokine receptor activity / complement receptor mediated signaling pathway / negative regulation of interleukin-12 production / Class A/1 (Rhodopsin-like receptors) / negative regulation of NF-kappaB transcription factor activity / positive regulation of macrophage chemotaxis / positive regulation of fat cell differentiation ...adipokinetic hormone binding / adipokinetic hormone receptor activity / complement receptor activity / chemokine receptor activity / complement receptor mediated signaling pathway / negative regulation of interleukin-12 production / Class A/1 (Rhodopsin-like receptors) / negative regulation of NF-kappaB transcription factor activity / positive regulation of macrophage chemotaxis / positive regulation of fat cell differentiation / regulation of calcium-mediated signaling / skeletal system development / G protein-coupled receptor activity / electron transport chain / chemotaxis / signaling receptor activity / positive regulation of cold-induced thermogenesis / positive regulation of cytosolic calcium ion concentration / phospholipase C-activating G protein-coupled receptor signaling pathway / periplasmic space / electron transfer activity / immune response / G protein-coupled receptor signaling pathway / inflammatory response / iron ion binding / heme binding / membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | |||||||||||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å | |||||||||||||||||||||
![]() | Zhu, Y. / He, M. / Wu, B. / Zhao, Q. | |||||||||||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural insights into the distinct ligand recognition and signaling of the chemerin receptors CMKLR1 and GPR1. Authors: Xiaowen Lin / Lechen Zhao / Heng Cai / Xiaohua Chang / Yuxuan Tang / Tianyu Luo / Mengdan Wu / Cuiying Yi / Limin Ma / Xiaojing Chu / Shuo Han / Qiang Zhao / Beili Wu / Maozhou He / Ya Zhu / ![]() | |||||||||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 149.2 KB | Display | ![]() |
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PDB format | ![]() | 108.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 380.3 KB | Display | ![]() |
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Full document | ![]() | 385.1 KB | Display | |
Data in XML | ![]() | 14.6 KB | Display | |
Data in CIF | ![]() | 22.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 62799MC ![]() 9l3wC ![]() 9l3yC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Antibody | Mass: 26917.025 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Antibody | Mass: 23586.205 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Protein | Mass: 56102.949 Da / Num. of mol.: 1 / Mutation: F259D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: CMKLR1, CHEMR23, DEZ, cybC / Production host: ![]() ![]() |
#4: Protein/peptide | Mass: 842.918 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
Has ligand of interest | Y |
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: CMKLR1 with ICL3-BRIL complex with anti-BRIL Fab and the antagonist LRH7-C2 Type: COMPLEX / Entity ID: #2-#3 / Source: RECOMBINANT | ||||||||||||||||
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Source (natural) |
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Source (recombinant) | Organism: ![]() ![]() | ||||||||||||||||
Buffer solution | pH: 7.5 | ||||||||||||||||
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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1500 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 70 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.20.1_4487 / Category: model refinement |
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CTF correction | Type: NONE |
3D reconstruction | Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 260967 / Symmetry type: POINT |
Refinement | Highest resolution: 3.9 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) |