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- PDB-2l4t: GIP/Glutaminase L peptide complex -

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Basic information

Entry
Database: PDB / ID: 2l4t
TitleGIP/Glutaminase L peptide complex
Components
  • Glutaminase L peptide
  • Tax1-binding protein 3
KeywordsPROTEIN BINDING / GIP / Glutaminase L / PDZ domain
Function / homology
Function and homology information


negative regulation of protein localization to cell surface / RHO GTPases Activate Rhotekin and Rhophilins / activation of GTPase activity / negative regulation of Wnt signaling pathway / Rho protein signal transduction / Wnt signaling pathway / fibrillar center / beta-catenin binding / actin cytoskeleton / negative regulation of cell population proliferation ...negative regulation of protein localization to cell surface / RHO GTPases Activate Rhotekin and Rhophilins / activation of GTPase activity / negative regulation of Wnt signaling pathway / Rho protein signal transduction / Wnt signaling pathway / fibrillar center / beta-catenin binding / actin cytoskeleton / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / extracellular exosome / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Tax1-binding protein 3 / : / PDZ domain / Pdz3 Domain / PDZ domain / PDZ domain profile. / Domain present in PSD-95, Dlg, and ZO-1/2. / PDZ domain / PDZ superfamily / Roll / Mainly Beta
Similarity search - Domain/homology
Tax1-binding protein 3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / DGSA-distance geometry simulated annealing
AuthorsZoetewey, D.L. / Ovee, M. / Banerjee, M. / Bhaskaran, R. / Mohanty, S.
CitationJournal: Biochemistry / Year: 2011
Title: Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L.
Authors: Zoetewey, D.L. / Ovee, M. / Banerjee, M. / Bhaskaran, R. / Mohanty, S.
History
DepositionOct 13, 2010Deposition site: BMRB / Processing site: RCSB
Revision 1.0Apr 6, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tax1-binding protein 3
B: Glutaminase L peptide


Theoretical massNumber of molelcules
Total (without water)14,7022
Polymers14,7022
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)20 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Tax1-binding protein 3 / Glutaminase-interacting protein 3 / Tax interaction protein 1 / TIP-1


Mass: 13751.685 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TAX1BP3, TIP1 / Plasmid: pET-3c/GIP / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): pLysS / References: UniProt: O14907
#2: Protein/peptide Glutaminase L peptide


Mass: 950.088 Da / Num. of mol.: 1 / Source method: obtained synthetically

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D HN(CA)CB
1413D CBCA(CO)NH
1513D C(CO)NH
1613D H(CCO)NH
1713D 1H-15N TOCSY
1813D (H)CCH-TOCSY
1913D 1H-15N NOESY
11013D 1H-13C NOESY
11113D 1H-13C FILTERED NOESY
11213D 1H-15N FILTERED NOESY

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Sample preparation

DetailsContents: 0.5-1 mM [U-99% 13C; U-99% 15N] Glutaminase Interacting Protein 3, 1-3 mM Glutaminase L peptide, 50 mM sodium phosphate, 0.1% w/v sodium azide, 1 mM EDTA, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)UnitsComponentIsotopic labelingConc. range (mg/ml)Solution-ID
mMGlutaminase Interacting Protein 3[U-99% 13C; U-99% 15N]0.5-11
mMGlutaminase L peptide1-31
50 mMsodium phosphate1
0.1 w/vsodium azide1
1 mMEDTA1
Sample conditionsIonic strength: 50 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE6001
Bruker AvanceBrukerAVANCE6002
Bruker AvanceBrukerAVANCE6003
Varian INOVAVarianINOVA5004

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Processing

NMR software
NameVersionDeveloperClassification
ARIA1.1Nilges, M. et al.data analysis
ARIA1.1Nilges, M. et al.refinement
RefinementMethod: DGSA-distance geometry simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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