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- PDB-1dzc: High resolution structure of acidic fibroblast growth factor. Mut... -

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Basic information

Entry
Database: PDB / ID: 1dzc
TitleHigh resolution structure of acidic fibroblast growth factor. Mutant FGF-4-ALA-(24-154), 24 NMR structures
ComponentsFIBROBLAST GROWTH FACTOR 1
KeywordsCELL CYCLE / GROWTH FACTOR / ANTITUMORAL
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 / regulation of endothelial cell chemotaxis to fibroblast growth factor / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / FGFR2b ligand binding and activation / positive regulation of cholesterol biosynthetic process ...mesonephric epithelium development / branch elongation involved in ureteric bud branching / regulation of endothelial tube morphogenesis / FGFR3b ligand binding and activation / regulation of endothelial cell chemotaxis to fibroblast growth factor / Signaling by activated point mutants of FGFR3 / FGFR3c ligand binding and activation / Phospholipase C-mediated cascade; FGFR3 / FGFR2b ligand binding and activation / positive regulation of cholesterol biosynthetic process / fibroblast growth factor receptor binding / FGFR2c ligand binding and activation / Activated point mutants of FGFR2 / Phospholipase C-mediated cascade; FGFR2 / 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:FGFR3 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / positive regulation of sprouting angiogenesis / PI-3K cascade:FGFR1 / positive regulation of cell division / PI3K Cascade / anatomical structure morphogenesis / fibroblast growth factor receptor signaling pathway / SHC-mediated cascade:FGFR3 / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / SHC-mediated cascade:FGFR1 / FRS-mediated FGFR3 signaling / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / FRS-mediated FGFR1 signaling / Signaling by FGFR2 in disease / Signaling by FGFR1 in disease / regulation of cell migration / activation of protein kinase B activity / Hsp70 protein binding / positive regulation of endothelial cell migration / extracellular matrix / epithelial cell proliferation / animal organ morphogenesis / Negative regulation of FGFR3 signaling / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / lung development / Negative regulation of FGFR1 signaling / positive regulation of MAP kinase activity / growth factor activity / wound healing / positive regulation of angiogenesis / Constitutive Signaling by Aberrant PI3K in Cancer / integrin binding / PIP3 activates AKT signaling / heparin binding / cellular response to heat / cell cortex / 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
HBGF/FGF family signature. / Fibroblast growth factor family / Fibroblast growth factor / Acidic and basic fibroblast growth factor family. / Cytokine IL1/FGF / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Mainly Beta
Similarity search - Domain/homology
Fibroblast growth factor 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS
AuthorsLozano, R.M. / Pineda-Lucena, A. / Gonzalez, C. / Jimenez, M.A. / Cuevas, P. / Redondo-Horcajo, M. / Sanz, J.M. / Rico, M. / Gimenez-Gallego, G.
CitationJournal: Biochemistry / Year: 2000
Title: 1H-NMR Structural Characterization of a Non Mitogenic, Vasodilatory, Ischemia-Protector and Neuromodulatory Acidic Fibroblast Growth Factor
Authors: Lozano, R.M. / Pineda-Lucena, A. / Gonzalez, C. / Jimenez, M.A. / Cuevas, P. / Redonde-Horcajo, M. / Sanz, J.M. / Rico, M. / Gimenez-Gallego, G.
History
DepositionFeb 24, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 16, 2000Provider: repository / Type: Initial release
Revision 1.1May 15, 2013Group: Derived calculations / Other ...Derived calculations / Other / Structure summary / Version format compliance
Revision 1.2May 15, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: FIBROBLAST GROWTH FACTOR 1


Theoretical massNumber of molelcules
Total (without water)14,6831
Polymers14,6831
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / 24
Representative

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Components

#1: Protein FIBROBLAST GROWTH FACTOR 1 / FGF-1 / ACIDIC FIBROBLAST GROWTH FACTOR / AFGF / ECGF / HBGF-1 / ENDOTHELIAL CELL GROWTH FACTOR / ...FGF-1 / ACIDIC FIBROBLAST GROWTH FACTOR / AFGF / ECGF / HBGF-1 / ENDOTHELIAL CELL GROWTH FACTOR / HEPARIN-BINDING GROWTH FACTOR 1


Mass: 14683.448 Da / Num. of mol.: 1 / Fragment: RESIDUES 25-155 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PMG624A / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P05230
Compound detailsCHAIN A: MUTATION: RESIDUES 24,25,26 SUBSTITUTED FOR ALA

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131COSY

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Sample preparation

DetailsContents: WATER
Sample conditionspH: 6 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
GROMOSVAN GUNSTEREN,BERENDSENrefinement
GROMOSstructure solution
RefinementMethod: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformers calculated total number: 24 / Conformers submitted total number: 24

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