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- PDB-1mhp: Crystal structure of a chimeric alpha1 integrin I-domain in compl... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mhp | ||||||
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Title | Crystal structure of a chimeric alpha1 integrin I-domain in complex with the Fab fragment of a humanized neutralizing antibody | ||||||
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![]() | IMMUNE SYSTEM / integrin / cell adhesion / receptor / antibody | ||||||
Function / homology | ![]() Integrin cell surface interactions / Smooth Muscle Contraction / cellular extravasation / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / basal part of cell / integrin complex / cell adhesion mediated by integrin / negative regulation of epidermal growth factor receptor signaling pathway / positive regulation of phosphoprotein phosphatase activity ...Integrin cell surface interactions / Smooth Muscle Contraction / cellular extravasation / integrin alpha1-beta1 complex / collagen binding involved in cell-matrix adhesion / basal part of cell / integrin complex / cell adhesion mediated by integrin / negative regulation of epidermal growth factor receptor signaling pathway / positive regulation of phosphoprotein phosphatase activity / collagen binding / neutrophil chemotaxis / cell-matrix adhesion / neuron projection morphogenesis / cell chemotaxis / acrosomal vesicle / integrin-mediated signaling pathway / cell-cell adhesion / vasodilation / positive regulation of neuron apoptotic process / integrin binding / perikaryon / protein phosphatase binding / positive regulation of MAPK cascade / cell adhesion / negative regulation of cell population proliferation / external side of plasma membrane / focal adhesion / signaling receptor binding / cell surface / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Karpusas, M. / Taylor, F. / Ferrant, J. / Weinreb, P. / Garber, E. | ||||||
![]() | ![]() Title: Crystal Structure of the alpha 1 beta 1 Integrin I Domain in Complex with an Antibody Fab Fragment Authors: Karpusas, M. / Ferrant, J. / Weinreb, P. / Carmillo, A. / Taylor, F. / Garber, E. | ||||||
History |
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Remark 999 | SEQUENCE AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS NOT AVAILABLE AT THE TIME OF PROCESSING FOR ...SEQUENCE AN APPROPRIATE SEQUENCE DATABASE REFERENCE WAS NOT AVAILABLE AT THE TIME OF PROCESSING FOR CHAINS H AND X (Fab fragment, heavy chain) AND FOR CHAINS L AND Y (FAB FRAGMENT, light chain). |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198.3 KB | Display | ![]() |
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PDB format | ![]() | 164.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.8 KB | Display | ![]() |
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Full document | ![]() | 516.4 KB | Display | |
Data in XML | ![]() | 41 KB | Display | |
Data in CIF | ![]() | 55.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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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: 21629.518 Da / Num. of mol.: 2 / Fragment: alpha1 I-domain / Mutation: G217V, R218Q, Q219R, L222R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Antibody | Mass: 23141.895 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Antibody | Mass: 23201.668 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.91 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PEG 1500, Tris, NaCl, beta-mercaptoethanol, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||||||||||||||||
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: Oct 5, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→35 Å / Num. all: 36501 / Num. obs: 35275 / % possible obs: 96.6 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Rmerge(I) obs: 0.083 / Net I/σ(I): 11.92 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 0.309 / Mean I/σ(I) obs: 2.29 / % possible all: 87.7 |
Reflection | *PLUS Lowest resolution: 500 Å |
Reflection shell | *PLUS % possible obs: 87.7 % |
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Processing
Software |
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.8→35 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 500 Å | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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