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- PDB-1qu0: CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qu0 | ||||||
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Title | CRYSTAL STRUCTURE OF THE FIFTH LAMININ G-LIKE MODULE OF THE MOUSE LAMININ ALPHA2 CHAIN | ||||||
![]() | LAMININ ALPHA2 CHAIN | ||||||
![]() | METAL BINDING PROTEIN / BETA SANDWICH / CALCIUM-BINDING PROTEIN | ||||||
Function / homology | ![]() regulation of basement membrane organization / Schwann cell differentiation / positive regulation of synaptic transmission, cholinergic / positive regulation of integrin-mediated signaling pathway / tissue development / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / positive regulation of muscle cell differentiation / regulation of embryonic development / positive regulation of cell adhesion ...regulation of basement membrane organization / Schwann cell differentiation / positive regulation of synaptic transmission, cholinergic / positive regulation of integrin-mediated signaling pathway / tissue development / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / positive regulation of muscle cell differentiation / regulation of embryonic development / positive regulation of cell adhesion / basement membrane / synaptic cleft / regulation of cell migration / substrate adhesion-dependent cell spreading / animal organ morphogenesis / axon guidance / neuromuscular junction / sarcolemma / collagen-containing extracellular matrix / dendritic spine / signaling receptor binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hohenester, E. / Tisi, D. / Talts, J.F. / Timpl, R. | ||||||
![]() | ![]() Title: The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin. Authors: Hohenester, E. / Tisi, D. / Talts, J.F. / Timpl, R. #1: ![]() Title: Structural analysis and proteolytic processing of recombinant G domain of mouse laminin alpha2 chain Authors: Talts, J.F. / Mann, K. / Yamada, Y. / Timpl, R. #2: ![]() Title: The role of laminins in basement membrane assembly Authors: Aumailley, M. / Smyth, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 149 KB | Display | ![]() |
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PDB format | ![]() | 122.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 464.5 KB | Display | ![]() |
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Full document | ![]() | 471.5 KB | Display | |
Data in XML | ![]() | 29.7 KB | Display | |
Data in CIF | ![]() | 41.3 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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3 | ![]()
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4 | ![]()
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Unit cell |
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Details | the asymmetric unit contains four copies of the laminin alpha2 LG5 module, which is monomeric in solution |
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Components
#1: Protein | Mass: 20420.248 Da / Num. of mol.: 4 / Fragment: LG5 MODULE Mutation: THE N-TERMINAL APLA SEQUENCE IS DERIVED FROM THE VECTOR Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.42 Å3/Da / Density % sol: 64.07 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 2 M ammonium sulfate, 2% isopropanol, 100 mM HEPES, 10 mM calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃Details: drop consists of equal volume 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: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 19, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.488 Å / Relative weight: 1 |
Reflection | Resolution: 2.35→20 Å / Num. all: 43258 / Num. obs: 43258 / % possible obs: 94.3 % / Observed criterion σ(I): 0 / Redundancy: 2.1 % / Biso Wilson estimate: 28 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 2.35→2.48 Å / Redundancy: 2 % / Rmerge(I) obs: 0.11 / % possible all: 85.8 |
Reflection shell | *PLUS % possible obs: 85.8 % |
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Processing
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Refinement | Resolution: 2.35→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber / Details: bulk solvent correction applied
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Refinement step | Cycle: LAST / Resolution: 2.35→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 41083 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |