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- PDB-1ckw: CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STR... -

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Basic information

Entry
Database: PDB / ID: 1ckw
TitleCYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR: SOLUTION STRUCTURES OF PEPTIDES BASED ON THE PHE508 REGION, THE MOST COMMON SITE OF DISEASE-CAUSING DELTA-F508 MUTATION
ComponentsPROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))
KeywordsMETAL TRANSPORT / P25_TFE / CYSTIC FIBROSIS / PEPTIDES
Function / homology
Function and homology information


Sec61 translocon complex binding / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / positive regulation of enamel mineralization / transepithelial water transport / intracellular pH elevation / amelogenesis / chloride channel inhibitor activity / multicellular organismal-level water homeostasis / cholesterol transport ...Sec61 translocon complex binding / channel-conductance-controlling ATPase / intracellularly ATP-gated chloride channel activity / positive regulation of enamel mineralization / transepithelial water transport / intracellular pH elevation / amelogenesis / chloride channel inhibitor activity / multicellular organismal-level water homeostasis / cholesterol transport / bicarbonate transport / bicarbonate transmembrane transporter activity / membrane hyperpolarization / vesicle docking involved in exocytosis / chloride transmembrane transporter activity / chloride channel activity / sperm capacitation / cholesterol biosynthetic process / positive regulation of exocytosis / positive regulation of insulin secretion involved in cellular response to glucose stimulus / chloride channel complex / ABC-type transporter activity / cellular response to cAMP / 14-3-3 protein binding / chloride transmembrane transport / cellular response to forskolin / response to endoplasmic reticulum stress / PDZ domain binding / isomerase activity / establishment of localization in cell / recycling endosome membrane / protein-folding chaperone binding / early endosome membrane / early endosome / chromatin extrusion motor activity / ATP-dependent H2AZ histone chaperone activity / cohesin loader activity / ATP-dependent H3-H4 histone complex chaperone activity / DNA clamp loader activity / apical plasma membrane / endoplasmic reticulum membrane / enzyme binding / cell surface / ATP hydrolysis activity / ATP binding / nucleus / membrane / plasma membrane / cytosol
Similarity search - Function
: / CFTR regulator domain / Cystic fibrosis TM conductance regulator (CFTR), regulator domain / Cystic fibrosis transmembrane conductance regulator / : / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site ...: / CFTR regulator domain / Cystic fibrosis TM conductance regulator (CFTR), regulator domain / Cystic fibrosis transmembrane conductance regulator / : / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Cystic fibrosis transmembrane conductance regulator
Similarity search - Component
MethodSOLUTION NMR / distance geometry
AuthorsMassiah, M.A. / Ko, Y.H. / Pedersen, P.L. / Mildvan, A.S.
CitationJournal: Biochemistry / Year: 1999
Title: Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation.
Authors: Massiah, M.A. / Ko, Y.H. / Pedersen, P.L. / Mildvan, A.S.
History
DepositionApr 26, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0May 4, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 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
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR))


Theoretical massNumber of molelcules
Total (without water)2,9071
Polymers2,9071
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)13 / 13LEAST RESTRAINTS VIOLATIONS AND LOW ENERGY
RepresentativeModel #1

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Components

#1: Protein/peptide PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR)) / P25


Mass: 2907.346 Da / Num. of mol.: 1 / Fragment: F508 MUTATION REGION / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE IS BASED ON THE PHE508 REGION OF CF TRANSMEMBRANE REGULATOR NUCLEOTIDE BINDING DOMAIN 1.
References: UniProt: Q00555

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121COSY
131TOCSY
NMR detailsText: THE SOLUTION STRUCTURES THE P25 (25 AMINO ACID FRAGMENT FROM THE CFTR NBD-1) PEPTIDE WERE DETERMINED IN 43% TRIFLUROETHANOL AND H2O BY HOMONUCLEAR 1H NMR SPECTROSCOPY PREFORMED ON A 600 MHZ ...Text: THE SOLUTION STRUCTURES THE P25 (25 AMINO ACID FRAGMENT FROM THE CFTR NBD-1) PEPTIDE WERE DETERMINED IN 43% TRIFLUROETHANOL AND H2O BY HOMONUCLEAR 1H NMR SPECTROSCOPY PREFORMED ON A 600 MHZ SPECTROMETER.. NOESY SPECTRA AT 100,200 AND 300 MS MIXING TIMES, TOCSY SPECTRUM AT 65 MS, AND COSY SPECTRUM WERE COLLECTED AND USED TO ASSIGN THE 1H RESONANCES AND NOES TO DETERMINE THE SOLUTION STRUCTURE

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Sample preparation

DetailsContents: 43% TRIFLUROETHANAL AND H2O
Sample conditionspH: 4 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.8BRUNGERrefinement
NMRVIEW2.1structure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINTS VIOLATIONS AND LOW ENERGY
Conformers calculated total number: 13 / Conformers submitted total number: 13

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