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Open data
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Basic information
Entry | Database: PDB / ID: 1i85 | ||||||
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Title | CRYSTAL STRUCTURE OF THE CTLA-4/B7-2 COMPLEX | ||||||
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Function / homology | ![]() positive regulation of lymphotoxin A production / protein complex involved in cell adhesion / CD40 signaling pathway / negative regulation of regulatory T cell differentiation / positive regulation of T-helper 2 cell differentiation / activation of protein kinase C activity / RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) / clathrin-coated endocytic vesicle / CD28 co-stimulation / CD28 dependent Vav1 pathway ...positive regulation of lymphotoxin A production / protein complex involved in cell adhesion / CD40 signaling pathway / negative regulation of regulatory T cell differentiation / positive regulation of T-helper 2 cell differentiation / activation of protein kinase C activity / RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) / clathrin-coated endocytic vesicle / CD28 co-stimulation / CD28 dependent Vav1 pathway / positive regulation of immunoglobulin production / CTLA4 inhibitory signaling / B cell activation / positive regulation of interleukin-4 production / negative regulation of B cell proliferation / Interleukin-10 signaling / CD28 dependent PI3K/Akt signaling / : / centriolar satellite / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schwartz, J.-C.D. / Zhang, X. / Fedorov, A.A. / Nathenson, S.G. / Almo, S.C. | ||||||
![]() | ![]() Title: Structural basis for co-stimulation by the human CTLA-4/B7-2 complex. Authors: Schwartz, J.C. / Zhang, X. / Fedorov, A.A. / Nathenson, S.G. / Almo, S.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92.8 KB | Display | ![]() |
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PDB format | ![]() | 77.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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Details | The CTLA-4 homodimer is generated by Chain D and the translatonal symmetry mate of chain C (apply the operator x,y,z+1 to Chain C) / The repeating arrangement of CTLA-4 and B7-2 dimers is generated by applying the translational symmetry operation (x,y,z+/-N; where N ranges over all integers) to all chains in the asymmetric unit |
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Components
#1: Antibody | Mass: 12849.631 Da / Num. of mol.: 2 / Fragment: IG V-TYPE (RECEPTOR BINDING) DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Protein | Mass: 13510.340 Da / Num. of mol.: 2 / Fragment: EXTRACELLULAR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||
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Crystal grow![]() | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG20K, HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||
Crystal grow | *PLUS Details: drop consists of equal amounts of protein and reservoir solutions | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 1, 2000 |
Radiation | Monochromator: NULL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 3.2→25 Å / Num. all: 7080 / Num. obs: 7080 / % possible obs: 78.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rmerge(I) obs: 0.121 / Net I/σ(I): 6.6 |
Reflection shell | Resolution: 3.2→3.31 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.321 / Mean I/σ(I) obs: 2.2 / % possible all: 79.4 |
Reflection shell | *PLUS % possible obs: 79.4 % |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Displacement parameters | Biso mean: 20.4 Å2 | |||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3.2→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.2→3.31 Å / Total num. of bins used: 10
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Xplor file | Serial no: 1 / Param file: protein_rep.param / Topol file: protein.top | |||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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