+Open data
-Basic information
Entry | Database: PDB / ID: 7yrr | ||||||
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Title | Cryo-EM structure of IGF1R with two IGF1 complex | ||||||
Components |
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Keywords | MEMBRANE PROTEIN / IGF1R-IGF1 | ||||||
Function / homology | Function and homology information glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / cardiac atrium development / negative regulation of cholangiocyte apoptotic process / proteoglycan biosynthetic process / positive regulation of glycoprotein biosynthetic process ...glycolate metabolic process / muscle hypertrophy / negative regulation of oocyte development / positive regulation of trophectodermal cell proliferation / insulin-like growth factor binding protein complex / insulin-like growth factor ternary complex / cardiac atrium development / negative regulation of cholangiocyte apoptotic process / proteoglycan biosynthetic process / positive regulation of glycoprotein biosynthetic process / myotube cell development / protein kinase complex / insulin-like growth factor receptor activity / positive regulation of steroid hormone biosynthetic process / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / negative regulation of neuroinflammatory response / Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R) / negative regulation of vascular associated smooth muscle cell apoptotic process / bone mineralization involved in bone maturation / insulin-like growth factor binding / IRS-related events triggered by IGF1R / protein transporter activity / positive regulation of cell growth involved in cardiac muscle cell development / exocytic vesicle / negative regulation of muscle cell apoptotic process / cellular response to progesterone stimulus / positive regulation of transcription regulatory region DNA binding / positive regulation of DNA metabolic process / cellular response to aldosterone / cellular response to zinc ion starvation / cell activation / positive regulation of calcineurin-NFAT signaling cascade / insulin receptor complex / insulin-like growth factor I binding / cellular response to testosterone stimulus / transcytosis / insulin receptor activity / negative regulation of hepatocyte apoptotic process / alphav-beta3 integrin-IGF-1-IGF1R complex / response to alkaloid / cellular response to angiotensin / positive regulation of Ras protein signal transduction / positive regulation of protein-containing complex disassembly / myoblast differentiation / positive regulation of insulin-like growth factor receptor signaling pathway / myoblast proliferation / dendritic spine maintenance / insulin binding / negative regulation of interleukin-1 beta production / response to L-glutamate / cellular response to insulin-like growth factor stimulus / muscle organ development / positive regulation of DNA binding / establishment of cell polarity / negative regulation of release of cytochrome c from mitochondria / positive regulation of cytokinesis / positive regulation of cardiac muscle hypertrophy / positive regulation of axon regeneration / positive regulation of smooth muscle cell migration / positive regulation of activated T cell proliferation / positive regulation of osteoblast proliferation / negative regulation of amyloid-beta formation / negative regulation of smooth muscle cell apoptotic process / amyloid-beta clearance / regulation of JNK cascade / Respiratory syncytial virus (RSV) attachment and entry / negative regulation of tumor necrosis factor production / insulin receptor substrate binding / epithelial to mesenchymal transition / positive regulation of glycogen biosynthetic process / G-protein alpha-subunit binding / Synthesis, secretion, and deacylation of Ghrelin / response to vitamin E / estrous cycle / negative regulation of MAPK cascade / SHC-related events triggered by IGF1R / positive regulation of osteoblast differentiation / phosphatidylinositol 3-kinase binding / peptidyl-tyrosine autophosphorylation / positive regulation of tyrosine phosphorylation of STAT protein / cellular response to transforming growth factor beta stimulus / positive regulation of vascular associated smooth muscle cell proliferation / insulin-like growth factor receptor binding / T-tubule / activation of protein kinase B activity / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of glycolytic process / positive regulation of mitotic nuclear division / axonogenesis / cellular response to dexamethasone stimulus / cerebellum development / positive regulation of epithelial cell proliferation / insulin-like growth factor receptor signaling pathway / platelet alpha granule lumen / skeletal system development / hippocampus development / cellular response to estradiol stimulus / positive regulation of D-glucose import / positive regulation of protein secretion / negative regulation of extrinsic apoptotic signaling pathway Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.3 Å | ||||||
Authors | Xi, Z. / Cang, W. | ||||||
Funding support | 1items
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Citation | Journal: To Be Published Title: Cryo-EM structure of IGF1R with two IGF1 complex at 4.3 angstroms resolution Authors: Xi, Z. / Cang, W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7yrr.cif.gz | 530.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7yrr.ent.gz | 438 KB | Display | PDB format |
PDBx/mmJSON format | 7yrr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7yrr_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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Full document | 7yrr_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 7yrr_validation.xml.gz | 60.5 KB | Display | |
Data in CIF | 7yrr_validation.cif.gz | 87.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yr/7yrr ftp://data.pdbj.org/pub/pdb/validation_reports/yr/7yrr | HTTPS FTP |
-Related structure data
Related structure data | 34065MC 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: 102424.906 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IGF1R / Cell line (production host): HEK293 / Production host: Homo sapiens (human) References: UniProt: P08069, receptor protein-tyrosine kinase #2: Protein | Mass: 6682.607 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IGF1 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P05019 Has protein modification | Y | |
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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 | Name: Deterotetramer complex of IGF1R with IGF1 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK293 |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: OTHER |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: OTHER |
Electron lens | Mode: OTHER / Nominal defocus max: 5000 nm / Nominal defocus min: 1200 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 4.3 Å / Resolution method: OTHER / Num. of particles: 100000 / Symmetry type: POINT | ||||||||||||||||||||||||
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