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- PDB-1pfl: REFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I -

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Entry
Database: PDB / ID: 1pfl
TitleREFINED SOLUTION STRUCTURE OF HUMAN PROFILIN I
ComponentsPROFILIN I
KeywordsREGULATORY PROTEIN
Function / homology
Function and homology information


synapse maturation / modification of postsynaptic actin cytoskeleton / negative regulation of actin filament bundle assembly / adenyl-nucleotide exchange factor activity / positive regulation of actin filament bundle assembly / negative regulation of actin filament polymerization / Signaling by ROBO receptors / regulation of actin filament polymerization / positive regulation of ATP-dependent activity / PCP/CE pathway ...synapse maturation / modification of postsynaptic actin cytoskeleton / negative regulation of actin filament bundle assembly / adenyl-nucleotide exchange factor activity / positive regulation of actin filament bundle assembly / negative regulation of actin filament polymerization / Signaling by ROBO receptors / regulation of actin filament polymerization / positive regulation of ATP-dependent activity / PCP/CE pathway / proline-rich region binding / positive regulation of ruffle assembly / negative regulation of stress fiber assembly / positive regulation of actin filament polymerization / positive regulation of epithelial cell migration / actin monomer binding / phosphatidylinositol-4,5-bisphosphate binding / phosphotyrosine residue binding / neural tube closure / RHO GTPases Activate Formins / modulation of chemical synaptic transmission / small GTPase binding / Platelet degranulation / actin binding / cell cortex / actin cytoskeleton organization / blood microparticle / protein stabilization / cytoskeleton / cadherin binding / focal adhesion / glutamatergic synapse / regulation of transcription by RNA polymerase II / RNA binding / extracellular exosome / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
Profilin1/2/3, vertebrate / : / Profilin conserved site / Profilin signature. / Profilin / Profilin / Profilin / Profilin superfamily / Dynein light chain 2a, cytoplasmic / Beta-Lactamase ...Profilin1/2/3, vertebrate / : / Profilin conserved site / Profilin signature. / Profilin / Profilin / Profilin / Profilin superfamily / Dynein light chain 2a, cytoplasmic / Beta-Lactamase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsMetzler, W.J. / Farmer II, B.T. / Constantine, K.L. / Friedrichs, M.S. / Lavoie, T. / Mueller, L.
Citation
#1: Journal: J.Biol.Chem. / Year: 1994
Title: Identification of the Poly-L-Proline-Binding Site on Human Profilin
Authors: Metzler, W.J. / Bell, A.J. / Ernst, E. / Lavoie, T.B. / Mueller, L.
#2: Journal: Biochemistry / Year: 1993
Title: Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N NMR Assignments and Global Folding Pattern
Authors: Metzler, W.J. / Constantine, K.L. / Friedrichs, M.S. / Bell, A.J. / Ernst, E.G. / Lavoie, T.B. / Mueller, L.
#3: Journal: FEBS Lett. / Year: 1993
Title: Relaxation Study of the Backbone Dynamics of Human Profilin by Two-Dimensional 1H-15N NMR
Authors: Constantine, K.L. / Friedrichs, M.S. / Bell, A.J. / Lavoie, T.B. / Mueller, L. / Metzler, W.J.
History
DepositionDec 12, 1994Processing site: BNL
Revision 1.0Mar 31, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4May 1, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROFILIN I


Theoretical massNumber of molelcules
Total (without water)14,9401
Polymers14,9401
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
Atom site foot note1: THE BACKBONE CONFORMATIONS OF THE FIRST TWO RESIDUES ARE NOT WELL CONSTRAINED BY THE NMR DATA.
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein PROFILIN I /


Mass: 14940.021 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line: BL-21 / Gene: HUMAN PROFILIN CDNA / Plasmid: PGPR-HUI (GENE IS UNDER CONTROL OF TRC PROMOT / Production host: Escherichia coli (E. coli) / References: UniProt: P07737

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 20

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