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

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Entry
Database: PDB / ID: 1ckz
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 / 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 / membrane hyperpolarization ...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 / membrane hyperpolarization / cholesterol transport / bicarbonate transport / bicarbonate transmembrane transporter activity / vesicle docking involved in exocytosis / chloride transmembrane transporter activity / sperm capacitation / chloride channel activity / 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 / cellular response to forskolin / chloride transmembrane transport / isomerase activity / response to endoplasmic reticulum stress / establishment of localization in cell / PDZ domain binding / recycling endosome membrane / early endosome membrane / protein-folding chaperone binding / early endosome / apical plasma membrane / endoplasmic reticulum membrane / enzyme binding / cell surface / ATP hydrolysis activity / ATP binding / membrane / nucleus / 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 / ABC transporters family signature. ...: / 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 / 50LEAST RESTRAINTS VIOLATIONS AND LOW ENERGY
RepresentativeModel #1

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Components

#1: Protein/peptide PROTEIN (CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR (CFTR)) / P25_H2O


Mass: 2907.346 Da / Num. of mol.: 1 / Fragment: P25, 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 OF THE PEPTIDE (P25) BASED ON THE PHE508 REGION OF CFTR WAS DETERMINED BY HOMONUCLEAR 1H NMR SPECTROSCOPY PERFORMED AT 600 MHZ. THE PEPTIDE WAS SYNTHETICALLY MADE AND ...Text: THE SOLUTION STRUCTURES OF THE PEPTIDE (P25) BASED ON THE PHE508 REGION OF CFTR WAS DETERMINED BY HOMONUCLEAR 1H NMR SPECTROSCOPY PERFORMED AT 600 MHZ. THE PEPTIDE WAS SYNTHETICALLY MADE AND WAS UNLABELED. 2D 1H NOESY SPECTRUM USING 100,200 AND 300 MIXING TIMES, 2D TOCSY AT 65 MS AND 2D COSY SPECTRA WERE COLLECTED WITH THE PEPTIDE IN 90%H2O/10%DMSO-D6.

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Sample preparation

DetailsContents: 90% WATER / 10% DMSO-D6
Sample conditionspH: 4.0 / 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: 50 / Conformers submitted total number: 13

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