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- PDB-7elj: Prion Derived Tetrapeptide Stabilizes Thermolabile Insulin via Co... -

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Basic information

Entry
Database: PDB / ID: 7elj
TitlePrion Derived Tetrapeptide Stabilizes Thermolabile Insulin via Conformational Trapping
Components
  • IS1
  • Insulin A Chain
  • Insulin B chain
KeywordsHORMONE / Insulin / Stabilization / Amyloid
Function / homology
Function and homology information


estradiol secretion / negative regulation of lactation / positive regulation of blood circulation / glucose import in response to insulin stimulus / positive regulation of cell maturation / positive regulation of lactation / response to L-arginine / positive regulation of mammary gland epithelial cell proliferation / negative regulation of appetite / response to butyrate ...estradiol secretion / negative regulation of lactation / positive regulation of blood circulation / glucose import in response to insulin stimulus / positive regulation of cell maturation / positive regulation of lactation / response to L-arginine / positive regulation of mammary gland epithelial cell proliferation / negative regulation of appetite / response to butyrate / response to food / feeding behavior / response to growth hormone / positive regulation of Rho protein signal transduction / positive regulation of peptide hormone secretion / protein secretion / response to glucose / negative regulation of lipid catabolic process / response to nutrient levels / positive regulation of protein secretion / insulin receptor binding / hormone activity / positive regulation of insulin secretion / glucose metabolic process / glucose homeostasis / response to heat / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of gene expression / negative regulation of apoptotic process / extracellular space / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin family signature. / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin-like superfamily
Similarity search - Domain/homology
Biological speciesBos taurus (cattle)
Homo sapiens (human)
MethodSOLUTION NMR / distance geometry
AuthorsBanerjee, N.
CitationJournal: Iscience / Year: 2021
Title: Prion-derived tetrapeptide stabilizes thermolabile insulin via conformational trapping.
Authors: Mukherjee, M. / Das, D. / Sarkar, J. / Banerjee, N. / Jana, J. / Bhat, J. / Reddy G, J. / Bharatam, J. / Chattopadhyay, S. / Chatterjee, S. / Chakrabarti, P.
History
DepositionApr 11, 2021Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 28, 2021Provider: repository / Type: Initial release
Revision 1.1Jul 7, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Insulin A Chain
B: Insulin B chain
C: IS1


Theoretical massNumber of molelcules
Total (without water)6,3443
Polymers6,3443
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area2530 Å2
ΔGint-20 kcal/mol
Surface area3720 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)8 / 10all calculated structures submitted
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Insulin A Chain


Mass: 2339.645 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P01317
#2: Protein/peptide Insulin B chain


Mass: 3403.927 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P01317
#3: Protein/peptide IS1


Mass: 600.687 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
112isotropic11D 1H
122isotropic12D 1H-1H NOESY
132isotropic23D 1H-15N NOESY

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Sample preparation

DetailsType: solution
Contents: 1 mM Proton Bovine Insulin, 1 mM Proton-15N, 13C Peptide, 90% H2O/10% D2O
Label: Insulin / Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMBovine InsulinProton2
1 mMPeptideProton-15N, 13C2
Sample conditionsIonic strength: 1 mM / Label: Condition_1 / pH: 2.6 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCE IIIBrukerAVANCE III5001
Bruker AVANCE IIIBrukerAVANCE III7002

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Processing

NMR software
NameVersionDeveloperClassification
TopSpin3.1Bruker Biospinrefinement
NMRFAM-SPARKYLee W, Tonelli M, Markley JLstructure calculation
TopSpinBruker Biospinchemical shift assignment
RefinementMethod: distance geometry / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: all calculated structures submitted
Conformers calculated total number: 10 / Conformers submitted total number: 8

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