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Open data
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Basic information
| Entry | Database: PDB / ID: 6wmw | ||||||
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| Title | GFRAL receptor bound with two antibody Fabs (3P10, 25M22) | ||||||
Components |
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Keywords | IMMUNE SYSTEM / RECEPTOR / SIGNALING / ANTIBODES | ||||||
| Function / homology | Function and homology informationresponse to metformin / glial cell-derived neurotrophic factor receptor activity / reduction of food intake in response to dietary excess / GDF15-GFRAL signaling pathway / negative regulation of appetite / stress-activated protein kinase signaling cascade / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / hormone activity / receptor tyrosine kinase binding / nervous system development ...response to metformin / glial cell-derived neurotrophic factor receptor activity / reduction of food intake in response to dietary excess / GDF15-GFRAL signaling pathway / negative regulation of appetite / stress-activated protein kinase signaling cascade / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / hormone activity / receptor tyrosine kinase binding / nervous system development / signaling receptor activity / actin cytoskeleton / negative regulation of neuron apoptotic process / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / positive regulation of MAPK cascade / external side of plasma membrane / focal adhesion / nucleoplasm / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.91 Å | ||||||
Authors | White, A. / Lakshminarasimhan, D. / Olland, A. / Suto, R.K. | ||||||
Citation | Journal: Nat Med / Year: 2020Title: Antibody-mediated inhibition of GDF15-GFRAL activity reverses cancer cachexia in mice. Authors: Suriben, R. / Chen, M. / Higbee, J. / Oeffinger, J. / Ventura, R. / Li, B. / Mondal, K. / Gao, Z. / Ayupova, D. / Taskar, P. / Li, D. / Starck, S.R. / Chen, H.H. / McEntee, M. / Katewa, S.D. ...Authors: Suriben, R. / Chen, M. / Higbee, J. / Oeffinger, J. / Ventura, R. / Li, B. / Mondal, K. / Gao, Z. / Ayupova, D. / Taskar, P. / Li, D. / Starck, S.R. / Chen, H.H. / McEntee, M. / Katewa, S.D. / Phung, V. / Wang, M. / Kekatpure, A. / Lakshminarasimhan, D. / White, A. / Olland, A. / Haldankar, R. / Solloway, M.J. / Hsu, J.Y. / Wang, Y. / Tang, J. / Lindhout, D.A. / Allan, B.B. | ||||||
| History |
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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 | 6wmw.cif.gz | 219 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6wmw.ent.gz | 171.6 KB | Display | PDB format |
| PDBx/mmJSON format | 6wmw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6wmw_validation.pdf.gz | 465.9 KB | Display | wwPDB validaton report |
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| Full document | 6wmw_full_validation.pdf.gz | 486.3 KB | Display | |
| Data in XML | 6wmw_validation.xml.gz | 37.5 KB | Display | |
| Data in CIF | 6wmw_validation.cif.gz | 51.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/6wmw ftp://data.pdbj.org/pub/pdb/validation_reports/wm/6wmw | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5vz4S S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| Unit cell |
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Components
| #1: Protein | Mass: 27665.693 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GFRAL, C6orf144, UNQ9356/PRO34128 / Production host: ![]() |
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| #2: Antibody | Mass: 24098.934 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #3: Antibody | Mass: 23745.457 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #4: Antibody | Mass: 24894.943 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #5: Antibody | Mass: 26652.068 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.81 % |
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| Crystal grow | Temperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1 M IMIDAZOLE Ph 7.0 AND 12% (w/w) peg 20,000 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.9774 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 23, 2016 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 0.9774 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.9→50 Å / Num. obs: 31586 / % possible obs: 99.6 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.099 / Rpim(I) all: 0.041 / Rrim(I) all: 0.108 / Χ2: 0.996 / Net I/σ(I): 10.2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 5vz4 Resolution: 2.91→47.7 Å / Cor.coef. Fo:Fc: 0.926 / Cor.coef. Fo:Fc free: 0.876 / SU B: 20.882 / SU ML: 0.39 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.446 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 209.9 Å2 / Biso mean: 75.054 Å2 / Biso min: 26.28 Å2
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| Refinement step | Cycle: final / Resolution: 2.91→47.7 Å
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| Refine LS restraints |
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| LS refinement shell | Resolution: 2.9→2.975 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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Homo sapiens (human)
X-RAY DIFFRACTION
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