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- PDB-2lgb: Modified A22Gly-B31Arg Human Insulin -

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Basic information

Entry
Database: PDB / ID: 2lgb
TitleModified A22Gly-B31Arg Human Insulin
Components
  • Insulin A chain
  • Insulin B chain
KeywordsHORMONE
Function / homology
Function and homology information


Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / Insulin processing / IRS activation / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of feeding behavior / negative regulation of fatty acid metabolic process ...Signaling by Insulin receptor / negative regulation of glycogen catabolic process / alpha-beta T cell activation / Insulin processing / IRS activation / Insulin receptor recycling / negative regulation of NAD(P)H oxidase activity / nitric oxide-cGMP-mediated signaling pathway / negative regulation of feeding behavior / negative regulation of fatty acid metabolic process / regulation of protein secretion / Regulation of gene expression in beta cells / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / negative regulation of respiratory burst involved in inflammatory response / positive regulation of dendritic spine maintenance / negative regulation of gluconeogenesis / negative regulation of reactive oxygen species biosynthetic process / positive regulation of lipid biosynthetic process / positive regulation of cellular protein metabolic process / Regulation of insulin secretion / negative regulation of protein secretion / COPI-mediated anterograde transport / Synthesis, secretion, and deacylation of Ghrelin / regulation of protein localization to plasma membrane / fatty acid homeostasis / positive regulation of glycogen biosynthetic process / regulation of cellular amino acid metabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / Signal attenuation / negative regulation of lipid catabolic process / endosome lumen / transport vesicle / positive regulation of insulin receptor signaling pathway / endoplasmic reticulum-Golgi intermediate compartment membrane / neuron projection maintenance / insulin-like growth factor receptor binding / positive regulation of protein autophosphorylation / regulation of transmembrane transporter activity / negative regulation of acute inflammatory response / positive regulation of glycolytic process / positive regulation of cell differentiation / Insulin receptor signalling cascade / regulation of synaptic plasticity / positive regulation of mitotic nuclear division / cognition / positive regulation of brown fat cell differentiation / regulation of protein localization / positive regulation of long-term synaptic potentiation / positive regulation of cytokine production / vasodilation / activation of protein kinase B activity / acute-phase response / positive regulation of glucose import / hormone activity / negative regulation of proteolysis / negative regulation of protein catabolic process / positive regulation of protein localization to nucleus / insulin receptor binding / insulin receptor signaling pathway / positive regulation of nitric-oxide synthase activity / glucose metabolic process / Golgi lumen / cell-cell signaling / glucose homeostasis / wound healing / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of MAPK cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / positive regulation of phosphatidylinositol 3-kinase signaling / secretory granule lumen / protease binding / positive regulation of NF-kappaB transcription factor activity / positive regulation of cell migration / positive regulation of protein kinase B signaling / Amyloid fiber formation / Golgi membrane / G protein-coupled receptor signaling pathway / amyloid fibril formation / endoplasmic reticulum lumen / regulation of transcription, DNA-templated / positive regulation of gene expression / positive regulation of cell population proliferation / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin / insulin-like growth factor / relaxin family. / Insulin/IGF/Relaxin family / Insulin, conserved site / Insulin-like superfamily / Insulin family signature.
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsBocian, W. / Kozerski, L.
CitationJournal: J.Biomol.Nmr / Year: 2012
Title: Recombinant A22(G)-B31 (R)-human insulin. A22 addition introduces conformational mobility in B chain C-terminus.
Authors: Borowicz, P. / Bednarek, E. / Bocian, W. / Sitkowski, J. / Jaworska, B. / Mikolajczyk, J. / Glabski, T. / Stadnik, D. / Surmacz, W. / Bogiel, M. / Kozerski, L.
History
DepositionJul 25, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Apr 11, 2012Provider: repository / Type: Initial release
Revision 1.1Jul 4, 2012Group: Structure summary

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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


Theoretical massNumber of molelcules
Total (without water)6,0322
Polymers6,0322
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 / 100structures with the lowest energy and with the least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Insulin A chain


Mass: 2440.750 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: INS / Production host: Escherichia coli (E. coli) / References: UniProt: P01308
#2: Protein/peptide Insulin B chain


Mass: 3591.146 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: INS / Production host: Escherichia coli (E. coli) / References: UniProt: P01308

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H TOCSY
1212D 1H-1H NOESY
1322D 1H-1H NOESY
1422D 1H-13C HSQC

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Sample preparation

Details
Solution-IDContentsSolvent system
13.0 - 2.0 mM Insulin A chain, 3.0 - 2.0 mM Insulin B chain, 65% H2O / 35% CD3CN65% H2O / 35% CD3CN
23.0 - 2.0 mM Insulin A chain, 3.0 - 2.0 mM Insulin B chain, 65% D2O / 35% CD3CN65% D2O / 35% CD3CN
Sample
UnitsComponentConc. range (mg/ml)Solution-ID
mMprotein_1-13.0-2.01
mMprotein_2-23.0-2.01
mMprotein_1-33.0-2.02
mMprotein_2-43.0-2.02
Sample conditionsIonic strength: 0 / pH: 3.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Varian Uniform NMR System / Manufacturer: Varian / Model: Uniform NMR System / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
AMBER9Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollmrefinement
AMBER9Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollmgeometry optimization
VNMRJ2.2CVariancollection
SPARKY2.6Goddardchemical shift assignment
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy and with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 20

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