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Yorodumi- PDB-4cmm: Structure of human CD47 in complex with human Signal Regulatory P... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4cmm | |||||||||
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Title | Structure of human CD47 in complex with human Signal Regulatory Protein (SIRP) alpha v1 | |||||||||
Components |
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Keywords | SIGNALING PROTEIN / PAIRED RECEPTOR / IMMUNOLOGICAL / INHIBITORY | |||||||||
Function / homology | Function and homology information negative regulation of I-kappaB phosphorylation / cellular response to interleukin-12 / monocyte extravasation / negative regulation of macrophage inflammatory protein 1 alpha production / regulation of Fc receptor mediated stimulatory signaling pathway / 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 / negative regulation of macrophage inflammatory protein 1 alpha production / regulation of Fc receptor mediated stimulatory signaling pathway / 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 / GTPase regulator activity / cell-cell adhesion mediator activity / regulation of interleukin-10 production / positive regulation of cell-cell adhesion / ATP export / 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 / regulation of interleukin-6 production / negative regulation of phagocytosis / Signal regulatory protein family interactions / thrombospondin receptor activity / negative regulation of interleukin-6 production / tertiary granule membrane / ficolin-1-rich granule membrane / negative regulation of tumor necrosis factor production / cellular response to interleukin-1 / negative regulation of cytokine production involved in inflammatory response / 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 type II interferon / negative regulation of inflammatory response / SH3 domain binding / cellular response to hydrogen peroxide / positive regulation of inflammatory response / positive regulation of reactive oxygen species metabolic process / positive regulation of T cell activation / cell migration / regulation of gene expression / cellular response to lipopolysaccharide / protein phosphatase binding / angiogenesis / cell adhesion / inflammatory response / positive regulation of cell population proliferation / Neutrophil degranulation / apoptotic process / cell surface / extracellular exosome / membrane / plasma membrane Similarity search - Function | |||||||||
Biological species | HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.92 Å | |||||||||
Authors | Hatherley, D. / Lea, S.M. / Johnson, S. / Barclay, A.N. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2014 Title: Polymorphisms in the Human Inhibitory Signal-Regulatory Protein Alpha Do not Affect Binding to its Ligand Cd47. Authors: Hatherley, D. / Lea, S.M. / Johnson, S. / Barclay, A.N. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4cmm.cif.gz | 66.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4cmm.ent.gz | 48.1 KB | Display | PDB format |
PDBx/mmJSON format | 4cmm.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4cmm_validation.pdf.gz | 453.8 KB | Display | wwPDB validaton report |
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Full document | 4cmm_full_validation.pdf.gz | 453.7 KB | Display | |
Data in XML | 4cmm_validation.xml.gz | 12.5 KB | Display | |
Data in CIF | 4cmm_validation.cif.gz | 17.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cm/4cmm ftp://data.pdbj.org/pub/pdb/validation_reports/cm/4cmm | HTTPS FTP |
-Related structure data
Related structure data | 2jjsS 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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Unit cell |
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-Components
#1: Protein | Mass: 14074.832 Da / Num. of mol.: 1 / Fragment: EXTRACELLULAR DOMAIN, RESIDUES 31-149 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 | ||||||
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#2: Antibody | Mass: 14518.302 Da / Num. of mol.: 1 / Fragment: EXTRACELLULAR DOMAIN, 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: Water | ChemComp-HOH / | Has protein modification | Y | Sequence details | CONTAINS C-TERMINAL HIS-TAG CONTAINS A C-TERMINAL HIS-TAG | |
-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: 48 % / Description: NONE |
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Crystal grow | pH: 8.5 / Details: 20% PEG 6000 0.1M TRIS PH8.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9793 |
Detector | Date: Jun 12, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9793 Å / Relative weight: 1 |
Reflection | Resolution: 1.92→34.62 Å / Num. obs: 21067 / % possible obs: 99.1 % / Observed criterion σ(I): 2 / Redundancy: 3.6 % / Biso Wilson estimate: 33.87 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 1.92→1.97 Å / Redundancy: 3 % / Rmerge(I) obs: 0.44 / Mean I/σ(I) obs: 2.5 / % possible all: 96 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2JJS Resolution: 1.92→34.62 Å / Cor.coef. Fo:Fc: 0.9247 / Cor.coef. Fo:Fc free: 0.9146 / SU R Cruickshank DPI: 0.15 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.156 / SU Rfree Blow DPI: 0.14 / SU Rfree Cruickshank DPI: 0.138
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Displacement parameters | Biso mean: 39.84 Å2
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Refinement step | Cycle: LAST / Resolution: 1.92→34.62 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.92→2.01 Å / Total num. of bins used: 11
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