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- PDB-2vxs: Structure of IL-17A in complex with a potent, fully human neutral... -
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Basic information
Entry | Database: PDB / ID: 2vxs | ||||||
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Title | Structure of IL-17A in complex with a potent, fully human neutralising antibody | ||||||
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![]() | CYTOKINE / EPITOPE / COMPLEX / ANTIBODY / SECRETED / GLYCOPROTEIN / INTERLEUKIN-17 | ||||||
Function / homology | ![]() positive regulation of interleukin-16 production / granulocyte migration / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / intestinal epithelial structure maintenance / negative regulation of inflammatory response to wounding / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / cell death / positive regulation of chemokine (C-X-C motif) ligand 1 production ...positive regulation of interleukin-16 production / granulocyte migration / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / intestinal epithelial structure maintenance / negative regulation of inflammatory response to wounding / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / cell death / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / positive regulation of bicellular tight junction assembly / fibroblast activation / positive regulation of osteoclast differentiation / positive regulation of cytokine production involved in inflammatory response / keratinocyte proliferation / cellular response to interleukin-1 / defense response to fungus / keratinocyte differentiation / Notch signaling pathway / positive regulation of interleukin-12 production / positive regulation of interleukin-1 beta production / cytokine activity / response to wounding / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / cell-cell signaling / gene expression / Interleukin-4 and Interleukin-13 signaling / defense response to Gram-negative bacterium / adaptive immune response / defense response to Gram-positive bacterium / inflammatory response / immune response / protein heterodimerization activity / external side of plasma membrane / innate immune response / apoptotic process / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gerhardt, S. / Hargreaves, D. / Pauptit, R.A. / Davies, R.A. / Russell, C. / Welsh, F. / Tuske, S.J. / Coales, S.J. / Hamuro, Y. / Needham, M.R.C. ...Gerhardt, S. / Hargreaves, D. / Pauptit, R.A. / Davies, R.A. / Russell, C. / Welsh, F. / Tuske, S.J. / Coales, S.J. / Hamuro, Y. / Needham, M.R.C. / Langham, C. / Barker, W. / Bell, P. / Aziz, A. / Smith, M.J. / Dawson, S. / Abbott, W.M. | ||||||
![]() | ![]() Title: Structure of Il-17A in Complex with a Potent, Fully Human Neutralising Antibody. Authors: Gerhardt, S. / Abbott, W.M. / Hargreaves, D. / Pauptit, R.A. / Davies, R.A. / Needham, M.R. / Langham, C. / Barker, W. / Aziz, A. / Snow, M.J. / Dawson, S. / Welsh, F. / Wilkinson, T. / ...Authors: Gerhardt, S. / Abbott, W.M. / Hargreaves, D. / Pauptit, R.A. / Davies, R.A. / Needham, M.R. / Langham, C. / Barker, W. / Aziz, A. / Snow, M.J. / Dawson, S. / Welsh, F. / Wilkinson, T. / Vaugan, T. / Beste, G. / Bishop, S. / Popovic, B. / Rees, G. / Sleeman, M. / Tuske, S.J. / Coales, S.J. / Hamuro, Y. / Russell, C. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 393.1 KB | Display | ![]() |
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PDB format | ![]() | 320.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 536.2 KB | Display | ![]() |
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Full document | ![]() | 577.4 KB | Display | |
Data in XML | ![]() | 69.9 KB | Display | |
Data in CIF | ![]() | 97.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1aqkS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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Components
#1: Protein | Mass: 15689.864 Da / Num. of mol.: 4 / Fragment: RESIDUES 20-155 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Antibody | Mass: 23671.508 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #3: Antibody | Mass: 23196.564 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #4: Chemical | ChemComp-SO4 / #5: Water | ChemComp-HOH / | Sequence details | SWISSPROT ACCESSION NUMBER Q16552. THE NUMBERING OF THE FAB-FRAGMENT (CHAINS H,I,J,K AND L,M,N,O) ...SWISSPROT ACCESSION NUMBER Q16552. THE NUMBERING OF THE FAB-FRAGMENT (CHAINS H,I,J,K AND L,M,N,O) ARE ACCORDING TO THE NOMENCLATU | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54 % / Description: NONE |
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Crystal grow | Details: 90.9 MM PCTP BUFFER PH 4.0, 9.1 MM PCTP BUFFER PH 9.5, 100 MM AMMONIUM SULPHATE, 14% W/V PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 30, 2007 / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9787 Å / Relative weight: 1 |
Reflection | Resolution: 2.63→102.1 Å / Num. obs: 79235 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 7 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 2.63→2.77 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 3.7 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1AQK Resolution: 2.63→204.12 Å / Cor.coef. Fo:Fc: 0.914 / Cor.coef. Fo:Fc free: 0.868 / SU B: 24.577 / SU ML: 0.236 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.635 / ESU R Free: 0.323 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.U VALUES RESIDUAL ONLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.75 Å2
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Refinement step | Cycle: LAST / Resolution: 2.63→204.12 Å
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Refine LS restraints |
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