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- PDB-1mhj: SOLUTION STRUCTURE OF THE SUPERACTIVE MONOMERIC DES-[PHE(B25)] HU... -

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Entry
Database: PDB / ID: 1mhj
TitleSOLUTION STRUCTURE OF THE SUPERACTIVE MONOMERIC DES-[PHE(B25)] HUMAN INSULIN MUTANT. ELUCIDATION OF THE STRUCTURAL BASIS FOR THE MONOMERIZATION OF THE DES-[PHE(B25)] INSULIN AND THE DIMERIZATION OF NATIVE INSULIN
Components(INSULIN) x 2
KeywordsHORMONE
Function / homology
Function and homology information


negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of peptide hormone secretion ...negative regulation of NAD(P)H oxidase activity / negative regulation of glycogen catabolic process / positive regulation of nitric oxide mediated signal transduction / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / Signaling by Insulin receptor / IRS activation / Insulin processing / regulation of protein secretion / positive regulation of peptide hormone secretion / positive regulation of respiratory burst / negative regulation of acute inflammatory response / Regulation of gene expression in beta cells / alpha-beta T cell activation / regulation of amino acid metabolic process / negative regulation of respiratory burst involved in inflammatory response / negative regulation of protein secretion / positive regulation of dendritic spine maintenance / positive regulation of glycogen biosynthetic process / Synthesis, secretion, and deacylation of Ghrelin / regulation of protein localization to plasma membrane / fatty acid homeostasis / negative regulation of gluconeogenesis / negative regulation of lipid catabolic process / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / COPI-mediated anterograde transport / positive regulation of lipid biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of insulin receptor signaling pathway / nitric oxide-cGMP-mediated signaling / negative regulation of reactive oxygen species biosynthetic process / positive regulation of protein autophosphorylation / Insulin receptor recycling / transport vesicle / insulin-like growth factor receptor binding / neuron projection maintenance / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of brown fat cell differentiation / positive regulation of protein metabolic process / NPAS4 regulates expression of target genes / activation of protein kinase B activity / positive regulation of glycolytic process / Insulin receptor signalling cascade / positive regulation of mitotic nuclear division / positive regulation of nitric-oxide synthase activity / positive regulation of cytokine production / positive regulation of long-term synaptic potentiation / acute-phase response / endosome lumen / Regulation of insulin secretion / positive regulation of D-glucose import / positive regulation of protein secretion / negative regulation of proteolysis / positive regulation of cell differentiation / regulation of transmembrane transporter activity / insulin receptor binding / wound healing / regulation of synaptic plasticity / negative regulation of protein catabolic process / hormone activity / positive regulation of neuron projection development / cognition / positive regulation of protein localization to nucleus / Golgi lumen / vasodilation / glucose metabolic process / cell-cell signaling / insulin receptor signaling pathway / glucose homeostasis / regulation of protein localization / positive regulation of NF-kappaB transcription factor activity / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / protease binding / secretory granule lumen / positive regulation of MAPK cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of cell migration / G protein-coupled receptor signaling pathway / Amyloid fiber formation / endoplasmic reticulum lumen / Golgi membrane / negative regulation of gene expression / positive regulation of cell population proliferation / regulation of DNA-templated transcription / positive regulation of gene expression / extracellular space / extracellular region / identical protein binding
Similarity search - Function
Insulin / Insulin family / Insulin-like / Insulin/IGF/Relaxin family / Insulin / insulin-like growth factor / relaxin family. / Insulin, conserved site / Insulin family signature. / Insulin-like superfamily
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsJorgensen, A.M.M. / Olsen, H.B. / Led, J.J. / Balschmidt, P.
Citation
Journal: J.Mol.Biol. / Year: 1996
Title: Solution structure of the superactive monomeric des-[Phe(B25)] human insulin mutant: elucidation of the structural basis for the monomerization of des-[Phe(B25)] insulin and the dimerization of native insulin.
Authors: Jorgensen, A.M. / Olsen, H.B. / Balschmidt, P. / Led, J.J.
#1: Journal: Magn.Reson.Chem. / Year: 1995
Title: A Carbon-13 NMR Study of the B9(Asp) Mutant of Human Insulin
Authors: Kristensen, S.M. / Led, J.J.
#2: Journal: Biochemistry / Year: 1994
Title: Structural Details of Asp(B9) Human Insulin at Low Ph from 2D NMR Titration Studies
Authors: Sorensen, M.D. / Led, J.J.
#3: Journal: J.Am.Chem.Soc. / Year: 1994
Title: A New Linear Prediction Model Method for the Determination of Slow Amide Proton Exchange Rates from a Series of One-Dimensional 1H NMR Spectra
Authors: Moss, R. / Gesmar, H. / Led, J.J.
#4: Journal: J.Am.Chem.Soc. / Year: 1993
Title: Slow Amide Proton Exchange Rates from the Line Widths in a Single Two-Dimensional 1H NMR Spectrum
Authors: Olsen, H.B. / Gesmar, H. / Led, J.J.
#5: Journal: J.Mol.Biol. / Year: 1992
Title: Three-Dimensional Solution Structure of an Insulin Dimer. A Study of the B9(Asp) Mutant of Human Insulin Using Nuclear Magnetic Resonance Distance Geometry and Restrained Molecular Dynamics
Authors: Jorgensen, A.M.M. / Kristensen, S.M. / Led, J.J. / Balschmidt, P.
#6: Journal: J.Mol.Biol. / Year: 1991
Title: Proton Nuclear Magnetic Resonance Study of the B9(Asp) Mutant of Human Insulin. Sequential Assignment and Secondary Structure
Authors: Kristensen, S.M. / Jorgensen, A.M.M. / Led, J.J. / Balschmidt, P. / Hansen, F.B.
History
DepositionNov 30, 1994Processing site: BNL
Revision 1.0Oct 15, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Oct 16, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: INSULIN
B: INSULIN


Theoretical massNumber of molelcules
Total (without water)5,6702
Polymers5,6702
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: THR B 26 - PRO B 27 MODEL 19 OMEGA = 211.56 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / -
Representative

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Components

#1: Protein/peptide INSULIN


Mass: 2383.698 Da / Num. of mol.: 1 / Mutation: DES-[PHE(B 25)]
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01308
#2: Protein/peptide INSULIN


Mass: 3286.779 Da / Num. of mol.: 1 / Mutation: DES-[PHE(B 25)]
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P01308
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR software
NameVersionDeveloperClassification
DISGEOHAVEL,WUTHRICHrefinement
X-PLOR2.1BRUNGERrefinement
NMR ensembleConformers submitted total number: 20

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