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Yorodumi- PDB-1apj: NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-... -
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-Basic information
Entry | Database: PDB / ID: 1apj | ||||||
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Title | NMR STUDY OF THE TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN (TB MODULE/8-CYS DOMAIN), NMR, 21 STRUCTURES | ||||||
Components | FIBRILLIN | ||||||
Keywords | EXTRACELLULAR MATRIX / FIBRILLIN FRAGMENT / MICROFIBRIL / TB MODULE / MARFAN SYNDROME / CONNECTIVE TISSUE / NOVEL FOLD | ||||||
Function / homology | Function and homology information post-embryonic eye morphogenesis / extracellular matrix constituent conferring elasticity / sequestering of BMP in extracellular matrix / sequestering of TGFbeta in extracellular matrix / microfibril / embryonic eye morphogenesis / negative regulation of osteoclast development / Elastic fibre formation / metanephros development / camera-type eye development ...post-embryonic eye morphogenesis / extracellular matrix constituent conferring elasticity / sequestering of BMP in extracellular matrix / sequestering of TGFbeta in extracellular matrix / microfibril / embryonic eye morphogenesis / negative regulation of osteoclast development / Elastic fibre formation / metanephros development / camera-type eye development / Molecules associated with elastic fibres / cellular response to insulin-like growth factor stimulus / cell adhesion mediated by integrin / extracellular matrix structural constituent / lung alveolus development / negative regulation of osteoclast differentiation / TGF-beta receptor signaling activates SMADs / basement membrane / anatomical structure morphogenesis / Integrin cell surface interactions / cellular response to transforming growth factor beta stimulus / Degradation of the extracellular matrix / extracellular matrix / skeletal system development / Post-translational protein phosphorylation / hormone activity / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / integrin binding / heart development / heparin binding / gene expression / collagen-containing extracellular matrix / endoplasmic reticulum lumen / calcium ion binding / protein-containing complex binding / extracellular space / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Yuan, X. / Downing, A.K. / Knott, V. / Handford, P.A. | ||||||
Citation | Journal: EMBO J. / Year: 1997 Title: Solution structure of the transforming growth factor beta-binding protein-like module, a domain associated with matrix fibrils. Authors: Yuan, X. / Downing, A.K. / Knott, V. / Handford, P.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1apj.cif.gz | 429.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1apj.ent.gz | 374.5 KB | Display | PDB format |
PDBx/mmJSON format | 1apj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ap/1apj ftp://data.pdbj.org/pub/pdb/validation_reports/ap/1apj | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8018.965 Da / Num. of mol.: 1 Fragment: TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN 6(TB6), RESIDUES 2054 - 2125 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Fragment: TRANSFORMING GROWTH FACTOR BETA BINDING PROTEIN-LIKE DOMAIN 6(TB6), RESIDUES 2054-2125 Plasmid: PQE30 / Production host: Escherichia coli (E. coli) / Strain (production host): NM554 / References: UniProt: P35555 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Crystal grow | *PLUS Method: other / Details: NMR |
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-Processing
Software |
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NMR software | Name: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement | ||||||||||||
NMR ensemble | Conformers submitted total number: 21 |