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- PDB-1t5q: Solution Structure of GIP(1-30)amide in TFE/Water -

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Basic information

Entry
Database: PDB / ID: 1t5q
TitleSolution Structure of GIP(1-30)amide in TFE/Water
ComponentsGastric inhibitory polypeptide
KeywordsHORMONE/GROWTH FACTOR / GIP / molecular modelling / helix / diabetes / obesity / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


gastric inhibitory polypeptide receptor binding / digestive system development / gastric inhibitory peptide signaling pathway / glucagon receptor binding / regulation of fatty acid biosynthetic process / positive regulation of cAMP-mediated signaling / Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) / endocrine pancreas development / response to selenium ion / response to acidic pH ...gastric inhibitory polypeptide receptor binding / digestive system development / gastric inhibitory peptide signaling pathway / glucagon receptor binding / regulation of fatty acid biosynthetic process / positive regulation of cAMP-mediated signaling / Synthesis, secretion, and inactivation of Glucose-dependent Insulinotropic Polypeptide (GIP) / endocrine pancreas development / response to selenium ion / response to acidic pH / positive regulation of glucose transmembrane transport / triglyceride homeostasis / exploration behavior / response to lipid / response to starvation / regulation of insulin secretion / response to axon injury / response to amino acid / response to glucose / sensory perception of pain / adult locomotory behavior / female pregnancy / long-term synaptic potentiation / adenylate cyclase-activating G protein-coupled receptor signaling pathway / positive regulation of insulin secretion / response to organic cyclic compound / hormone activity / memory / response to peptide hormone / Glucagon-type ligand receptors / G alpha (s) signalling events / secretory granule lumen / response to xenobiotic stimulus / endoplasmic reticulum lumen / neuronal cell body / signal transduction / extracellular space / extracellular region
Similarity search - Function
Gastric inhibitory polypeptide / Glucagon/GIP/secretin/VIP / Peptide hormone / Glucagon / GIP / secretin / VIP family signature. / Glucagon like hormones
Similarity search - Domain/homology
Gastric inhibitory polypeptide
Similarity search - Component
MethodSOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, CONJUGATE-GRADIENT MINIMISATION, POWELL MINIMISATION
AuthorsAlana, I. / Hewage, C.M. / Malthouse, J.P.G. / Parker, J.C. / Gault, V.A. / O'Harte, F.P.M.
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2004
Title: NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide.
Authors: Alana, I. / Hewage, C.M. / Malthouse, J.P.G. / Parker, J.C. / Gault, V.A. / O'Harte, F.P.M.
History
DepositionMay 5, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 16, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond
Remark 650HELIX determination method: author

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Gastric inhibitory polypeptide


Theoretical massNumber of molelcules
Total (without water)3,5361
Polymers3,5361
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 / 200CYANA target function
Representative

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Components

#1: Protein/peptide Gastric inhibitory polypeptide / GIP / Glucose-dependent insulinotropic polypeptide


Mass: 3535.954 Da / Num. of mol.: 1 / Fragment: residues 1-30 / Source method: obtained synthetically
Details: The peptide was chemically synthesized, the sequence of the peptide can be naturally found in Homo sapiens (Human)
References: UniProt: P09681

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111DQF-COSY
1212D TOCSY
1312D NOESY
1411D variable temperature
1511D D2O exchange
NMR detailsText: These structures were determined using standard 2D homonuclear techniques

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Sample preparation

DetailsContents: 2mM GIP(1-30)amide, 50% H2O, 50% d3-TFE / Solvent system: 50% H2O, 50% d3-TFE
Sample conditionspH: 3.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Bruker DRXBrukerDRX9002

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.5Brukercollection
XwinNMR3.5Brukerprocessing
SYBYL6.81Triposdata analysis
CYANA1.0.6Guentertstructure solution
SYBYL6.81Triposrefinement
RefinementMethod: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, CONJUGATE-GRADIENT MINIMISATION, POWELL MINIMISATION
Software ordinal: 1
NMR ensembleConformer selection criteria: CYANA target function / Conformers calculated total number: 200 / Conformers submitted total number: 20

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