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Yorodumi- PDB-2jjs: Structure of human CD47 in complex with human signal regulatory p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2jjs | |||||||||
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Title | Structure of human CD47 in complex with human signal regulatory protein (SIRP) alpha | |||||||||
Components |
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Keywords | CELL ADHESION / SIGNAL REGULATORY PROTEIN ALPHA / IMMUNOGLOBULIN SUPERFAMILY / TRANSMEMBRANE / PHOSPHOPROTEIN / PAIRED RECEPTOR / POLYMORPHISM / GLYCOPROTEIN / PYRROLIDONE CARBOXYLIC ACID / ALTERNATIVE SPLICING / IMMUNOGLOBULIN DOMAIN / SIRP / CD47 / SIRPA / MEMBRANE / SH3-BINDING | |||||||||
Function / homology | Function and homology information negative regulation of I-kappaB phosphorylation / cellular response to interleukin-12 / monocyte extravasation / regulation of Fc receptor mediated stimulatory signaling pathway / negative regulation of macrophage inflammatory protein 1 alpha production / negative regulation of chemokine (C-C motif) ligand 5 production / protein binding involved in heterotypic cell-cell adhesion / positive regulation of monocyte extravasation / regulation of interleukin-1 beta production / regulation of type II interferon production ...negative regulation of I-kappaB phosphorylation / cellular response to interleukin-12 / monocyte extravasation / regulation of Fc receptor mediated stimulatory signaling pathway / negative regulation of macrophage inflammatory protein 1 alpha production / negative regulation of chemokine (C-C motif) ligand 5 production / protein binding involved in heterotypic cell-cell adhesion / positive regulation of monocyte extravasation / regulation of interleukin-1 beta production / regulation of type II interferon production / cell-cell adhesion mediator activity / ATP export / GTPase regulator activity / positive regulation of cell-cell adhesion / regulation of interleukin-10 production / protein antigen binding / negative regulation of nitric oxide biosynthetic process / negative regulation of interferon-beta production / negative regulation of JNK cascade / regulation of tumor necrosis factor production / regulation of interleukin-12 production / regulation of nitric oxide biosynthetic process / negative regulation of phagocytosis / regulation of interleukin-6 production / Signal regulatory protein family interactions / thrombospondin receptor activity / tertiary granule membrane / negative regulation of interleukin-6 production / ficolin-1-rich granule membrane / negative regulation of tumor necrosis factor production / negative regulation of cytokine production involved in inflammatory response / cellular response to interleukin-1 / Integrin cell surface interactions / specific granule membrane / positive regulation of phagocytosis / positive regulation of stress fiber assembly / protein tyrosine kinase binding / negative regulation of protein phosphorylation / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / negative regulation of ERK1 and ERK2 cascade / cellular response to hydrogen peroxide / negative regulation of inflammatory response / SH3 domain binding / positive regulation of inflammatory response / cellular response to type II interferon / positive regulation of T cell activation / cell migration / regulation of gene expression / protein phosphatase binding / angiogenesis / cellular response to lipopolysaccharide / cell adhesion / inflammatory response / apoptotic process / positive regulation of cell population proliferation / Neutrophil degranulation / cell surface / extracellular exosome / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | |||||||||
Authors | Hatherley, D. / Graham, S.C. / Turner, J. / Harlos, K. / Stuart, D.I. / Barclay, A.N. | |||||||||
Citation | Journal: Mol. Cell / Year: 2008 Title: Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47. Authors: Hatherley, D. / Graham, S.C. / Turner, J. / Harlos, K. / Stuart, D.I. / Barclay, A.N. | |||||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | |||||||||
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. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jjs.cif.gz | 206.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jjs.ent.gz | 165.9 KB | Display | PDB format |
PDBx/mmJSON format | 2jjs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jj/2jjs ftp://data.pdbj.org/pub/pdb/validation_reports/jj/2jjs | HTTPS FTP |
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-Related structure data
Related structure data | 2jjtC 2jjuC 2jjvC 2jjwC 2vscC 2iccS 2uv3S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 13919.563 Da / Num. of mol.: 2 / Fragment: N-TERMINAL ECTODOMAIN, RESIDUES 31-148 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEE14 / Cell line (production host): CHO / Production host: CRICETULUS GRISEUS (Chinese hamster) / Variant (production host): LEC3.2.8.1 / References: UniProt: P78324 #2: Antibody | Mass: 14518.302 Da / Num. of mol.: 2 Fragment: IMMUNOGLOBULIN-SUPERFAMILY ECTODOMAIN, RESIDUES 19-136 Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PEE14 / Cell line (production host): CHO / Production host: CRICETULUS GRISEUS (Chinese hamster) / Variant (production host): LEC3.2.8.1 / References: UniProt: Q08722 #3: Sugar | ChemComp-NAG / #4: Chemical | ChemComp-IOD / #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | SIRP ALPHA (CHAINS A AND B) RESIDUE NUMBERING IS FOR THE MATURE PROTEIN (LACKING N-TERMINAL 30 ...SIRP ALPHA (CHAINS A AND B) RESIDUE NUMBERING IS FOR THE MATURE PROTEIN (LACKING N-TERMINAL 30 AMINO ACID SIGNAL SEQUENCE). C-TERMINAL PURIFICATI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 49.3 % / Description: NONE |
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Crystal grow | Temperature: 278 K / pH: 7.4 Details: 100 NL SIRP ALPHA / CD47 COMPLEX (1:1 RATIO, EACH PROTEIN AT APPROX. 0.375 UM) PLUS 100 NL RESERVOIR (0.2 M POTASSIUM IODIDE, 20% W/V PEG 3350) EQUILIBRATED AGAINST 95 UL OF RESERVOIR AT 5 C., pH 7.4 |
-Data collection
Diffraction |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 1.85→29.8 Å / Num. obs: 46373 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 10.3 % / Biso Wilson estimate: 19.5 Å2 / Rmerge(I) obs: 0.14 / Net I/σ(I): 17.6 | ||||||||||||||||||
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 9.2 % / Rmerge(I) obs: 0.79 / Mean I/σ(I) obs: 2.8 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2UV3 FOR CHAINS A AND B, PDB ENTRY 2ICC FOR CHAINS C AND D Resolution: 1.85→89.44 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.93 / SU B: 4.986 / SU ML: 0.085 / Cross valid method: THROUGHOUT / ESU R: 0.127 / ESU R Free: 0.125 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. B VALUES INCLUDE TLS CONTRIBUTIONS.
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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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.2 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→89.44 Å
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Refine LS restraints |
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