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- PDB-1kq8: Solution Structure of Winged Helix Protein HFH-1 -

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Basic information

Entry
Database: PDB / ID: 1kq8
TitleSolution Structure of Winged Helix Protein HFH-1
ComponentsHEPATOCYTE NUCLEAR FACTOR 3 FORKHEAD HOMOLOG 1
KeywordsTRANSCRIPTION / Winged Helix Protein / HFH-1
Function / homology
Function and homology information


hair follicle morphogenesis / anatomical structure morphogenesis / DNA-binding transcription repressor activity, RNA polymerase II-specific / negative regulation of neuron apoptotic process / cell differentiation / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / nucleus
Similarity search - Function
Fork head domain conserved site1 / Fork head domain signature 1. / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A ...Fork head domain conserved site1 / Fork head domain signature 1. / Fork head domain / Forkhead domain / Fork head domain profile. / FORKHEAD / Fork head domain conserved site 2 / Fork head domain signature 2. / Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain / Arc Repressor Mutant, subunit A / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Forkhead box protein Q1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsSheng, W. / Rance, M. / Liao, X.
Citation
Journal: Biochemistry / Year: 2002
Title: Structure comparison of two conserved HNF-3/fkh proteins HFH-1 and genesis indicates the existence of folding differences in their complexes with a DNA binding sequence.
Authors: Sheng, W. / Rance, M. / Liao, X.
#1: Journal: J.Mol.Biol. / Year: 1998
Title: Structural changes in the region directly adjacent to the DNA-binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins
Authors: Marsden, I. / Jin, C. / Liao, X.
#2: Journal: Biochemistry / Year: 1998
Title: Sequence specific collective motions in a winged helix DNA binding domain detected by 15N relaxation NMR
Authors: Jin, C. / Marsden, I. / Chen, X. / Liao, X.
History
DepositionJan 4, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 22, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HEPATOCYTE NUCLEAR FACTOR 3 FORKHEAD HOMOLOG 1


Theoretical massNumber of molelcules
Total (without water)11,8041
Polymers11,8041
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200target function
Representative

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Components

#1: Protein HEPATOCYTE NUCLEAR FACTOR 3 FORKHEAD HOMOLOG 1 / HFH-1 / HNF-3/forkhead homolog-1 / winged helix/forkhead transcription factor


Mass: 11804.493 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Production host: Escherichia coli (E. coli) / References: UniProt: Q63244

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
2223D 13C-separated NOESY
333HNCA-J
444HNHA

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Sample preparation

Sample conditionspH: 6.5 / Temperature: 290 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DMXBrukerDMX7502
Varian UNITYPLUSVarianUNITYPLUS8003

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Processing

NMR softwareName: DYANA / Version: 1.5 / Developer: Gunter, P. / Classification: refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20

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