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Yorodumi- PDB-1rml: NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rml | ||||||
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Title | NMR STUDY OF ACID FIBROBLAST GROWTH FACTOR BOUND TO 1,3,6-NAPHTHALENE TRISULPHONATE, 26 STRUCTURES | ||||||
Components | ACIDIC FIBROBLAST GROWTH FACTOR | ||||||
Keywords | GROWTH FACTOR / FIBROBLAST GROWTH FACTOR / ANTITUMORAL / NAPHTHALENE | ||||||
Function / homology | Function and homology information mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / FGFR3b ligand binding and activation / FGFR2b ligand binding and activation / regulation of endothelial cell chemotaxis to fibroblast growth factor / FGFR2c ligand binding and activation / Activated point mutants of FGFR2 / Phospholipase C-mediated cascade; FGFR2 / Signaling by activated point mutants of FGFR3 ...mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / FGFR3b ligand binding and activation / FGFR2b ligand binding and activation / regulation of endothelial cell chemotaxis to fibroblast growth factor / FGFR2c ligand binding and activation / Activated point mutants of FGFR2 / Phospholipase C-mediated cascade; FGFR2 / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / positive regulation of cholesterol biosynthetic process / fibroblast growth factor receptor binding / FGFR4 ligand binding and activation / FGFR1b ligand binding and activation / Phospholipase C-mediated cascade; FGFR4 / Signaling by activated point mutants of FGFR1 / organ induction / FGFR1c ligand binding and activation / Downstream signaling of activated FGFR1 / Phospholipase C-mediated cascade: FGFR1 / S100 protein binding / positive regulation of hepatocyte proliferation / positive regulation of intracellular signal transduction / Signaling by FGFR2 IIIa TM / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / positive regulation of sprouting angiogenesis / PI-3K cascade:FGFR1 / positive regulation of cell division / PI3K Cascade / fibroblast growth factor receptor signaling pathway / anatomical structure morphogenesis / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR3 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR2 signaling / FRS-mediated FGFR3 signaling / Signaling by FGFR2 in disease / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / FRS-mediated FGFR1 signaling / Signaling by FGFR1 in disease / Hsp70 protein binding / activation of protein kinase B activity / regulation of cell migration / positive regulation of endothelial cell migration / extracellular matrix / epithelial cell proliferation / animal organ morphogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR3 signaling / lung development / Negative regulation of FGFR4 signaling / Negative regulation of FGFR1 signaling / growth factor activity / positive regulation of MAP kinase activity / wound healing / positive regulation of angiogenesis / Constitutive Signaling by Aberrant PI3K in Cancer / integrin binding / PIP3 activates AKT signaling / heparin binding / cell cortex / cellular response to heat / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / RAF/MAP kinase cascade / angiogenesis / positive regulation of ERK1 and ERK2 cascade / cell differentiation / positive regulation of cell migration / positive regulation of cell population proliferation / positive regulation of gene expression / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / VARIABLE TARGET FUNCTION | ||||||
Authors | Lozano, R.M. / Jimenez, M.A. / Santoro, J. / Rico, M. / Gimenez-Gallego, G. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1998 Title: Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas. Authors: Lozano, R.M. / Jimenez, M. / Santoro, J. / Rico, M. / Gimenez-Gallego, G. #1: Journal: J.Mol.Biol. / Year: 1996 Title: Three-Dimensional Structure of Acidic Fibroblast Growth Factor in Solution: Effects of Binding to a Heparin Functional Analog Authors: Pineda-Lucena, A. / Jimenez, M.A. / Lozano, R.M. / Nieto, J.L. / Santoro, J. / Rico, M. / Gimenez-Gallego, G. #2: Journal: J.Mol.Biol. / Year: 1994 Title: 1H-NMR Assignment and Solution Structure of Human Acidic Fibroblast Growth Factor Activated by Inositol Hexasulfate Authors: Pineda-Lucena, A. / Jimenez, M.A. / Nieto, J.L. / Santoro, J. / Rico, M. / Gimenez-Gallego, G. #3: Journal: J.Mol.Biol. / Year: 1994 Title: Erratum. 1H-NMR Assignment and Solution Structure of Human Acidic Fibroblast Growth Factor Activated by Inositol Hexasulfate Authors: Pineda-Lucena, A. / Jimenez, M.A. / Nieto, J.L. / Santoro, J. / Rico, M. / Gimenez-Gallego, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rml.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1rml.ent.gz | 879.8 KB | Display | PDB format |
PDBx/mmJSON format | 1rml.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1rml_validation.pdf.gz | 447.7 KB | Display | wwPDB validaton report |
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Full document | 1rml_full_validation.pdf.gz | 785.9 KB | Display | |
Data in XML | 1rml_validation.xml.gz | 122.1 KB | Display | |
Data in CIF | 1rml_validation.cif.gz | 146.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rm/1rml ftp://data.pdbj.org/pub/pdb/validation_reports/rm/1rml | HTTPS FTP |
-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: 17482.697 Da / Num. of mol.: 1 / Fragment: RESIDUES 23 - 154 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PMG47 / Production host: Escherichia coli (E. coli) / References: UniProt: P05230 |
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#2: Chemical | ChemComp-NTS / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: WATER |
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Sample conditions | pH: 6 / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: VARIABLE TARGET FUNCTION / Software ordinal: 1 | |||||||||
NMR ensemble | Conformers calculated total number: 26 / Conformers submitted total number: 26 |