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- PDB-1hod: NMR STRUCTURE OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE FROM TH... -

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Basic information

Entry
Database: PDB / ID: 1hod
TitleNMR STRUCTURE OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE FROM THE ALPHA 2A ADRENERGIC RECEPTOR
ComponentsALPHA-2A ADRENERGIC RECEPTOR
KeywordsMEMBRANE PROTEIN / HELIX-LINKER-HELIX
Function / homology
Function and homology information


negative regulation of uterine smooth muscle contraction / adenylate cyclase-inhibiting adrenergic receptor signaling pathway / phospholipase C-activating adrenergic receptor signaling pathway / alpha2-adrenergic receptor activity / Adrenaline signalling through Alpha-2 adrenergic receptor / alpha-2C adrenergic receptor binding / receptor transactivation / epinephrine binding / alpha-1B adrenergic receptor binding / negative regulation of norepinephrine secretion ...negative regulation of uterine smooth muscle contraction / adenylate cyclase-inhibiting adrenergic receptor signaling pathway / phospholipase C-activating adrenergic receptor signaling pathway / alpha2-adrenergic receptor activity / Adrenaline signalling through Alpha-2 adrenergic receptor / alpha-2C adrenergic receptor binding / receptor transactivation / epinephrine binding / alpha-1B adrenergic receptor binding / negative regulation of norepinephrine secretion / negative regulation of calcium ion transmembrane transporter activity / negative regulation of epinephrine secretion / heterotrimeric G-protein binding / negative regulation of calcium ion-dependent exocytosis / fear response / dopaminergic synapse / Surfactant metabolism / positive regulation of potassium ion transport / thermoception / thioesterase binding / negative regulation of insulin secretion involved in cellular response to glucose stimulus / positive regulation of membrane protein ectodomain proteolysis / norepinephrine binding / Adrenoceptors / intestinal absorption / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of wound healing / activation of protein kinase activity / adrenergic receptor signaling pathway / negative regulation of calcium ion transport / Rho protein signal transduction / regulation of vasoconstriction / negative regulation of lipid catabolic process / negative regulation of insulin secretion / adenylate cyclase-activating adrenergic receptor signaling pathway / GABA-ergic synapse / presynaptic active zone membrane / axon terminus / cellular response to hormone stimulus / presynaptic modulation of chemical synaptic transmission / activation of protein kinase B activity / adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway / guanyl-nucleotide exchange factor activity / positive regulation of cytokine production / female pregnancy / postsynaptic density membrane / positive regulation of MAP kinase activity / adenylate cyclase-activating G protein-coupled receptor signaling pathway / platelet activation / Adrenaline,noradrenaline inhibits insulin secretion / G alpha (z) signalling events / vasodilation / glucose homeostasis / G alpha (i) signalling events / actin cytoskeleton organization / basolateral plasma membrane / Ras protein signal transduction / DNA replication / positive regulation of MAPK cascade / receptor complex / positive regulation of cell migration / protein heterodimerization activity / G protein-coupled receptor signaling pathway / neuronal cell body / glutamatergic synapse / positive regulation of cell population proliferation / protein kinase binding / protein homodimerization activity / plasma membrane / cytoplasm
Similarity search - Function
Alpha 2A adrenoceptor / Adrenoceptor family / Serpentine type 7TM GPCR chemoreceptor Srsx / G-protein coupled receptors family 1 signature. / G protein-coupled receptor, rhodopsin-like / GPCR, rhodopsin-like, 7TM / G-protein coupled receptors family 1 profile. / 7 transmembrane receptor (rhodopsin family)
Similarity search - Domain/homology
Alpha-2A adrenergic receptor
Similarity search - Component
MethodSOLUTION NMR / SIMULATED ANNEALING IN TORSION ANGLE SPACE
AuthorsChung, D.A. / Zuiderweg, E.R. / Neubig, R.R.
CitationJournal: Biochemistry / Year: 2002
Title: NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix.
Authors: Chung, D.A. / Zuiderweg, E.R. / Fowler, C.B. / Soyer, O.S. / Mosberg, H.I. / Neubig, R.R.
History
DepositionDec 10, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 24, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 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 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

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Assembly

Deposited unit
A: ALPHA-2A ADRENERGIC RECEPTOR


Theoretical massNumber of molelcules
Total (without water)3,7961
Polymers3,7961
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)1 / -
RepresentativeModel #1average structure

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Components

#1: Protein/peptide ALPHA-2A ADRENERGIC RECEPTOR / ALPHA-2A ADRENOCEPTOR


Mass: 3796.449 Da / Num. of mol.: 1 / Fragment: SECOND INTRACELLULAR LOOP (RESIDUES 118-149) / Mutation: D130I / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE OF THE PEPTIDE OCCURS NATURALLY IN HOMO SAPIENS (HUMAN).
References: UniProt: P08913

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
1312D COSY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.590% H2O/10% D2O
20.9 mM PEPTIDE NATURAL ABUNDANCE; 460 mM D38- DODECYLPHOSPHOCHOLINE, 50 mM NACL, 10 mM NAH2PO4, PH 4.5100 % D20
Sample conditions
Conditions-IDIonic strengthpHTemperature (K)
150 mM NACL 4.5303.00 K
250 mM 4.5303.00 K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz

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Processing

NMR software
NameDeveloperClassification
DYANAGuntertstructure solution
XEASYBartelsdata analysis
NMRPipeDelaglioprocessing
NMRViewJohnsonprocessing
SPSCANGlaserdata analysis
DYANAGuntertrefinement
RefinementMethod: SIMULATED ANNEALING IN TORSION ANGLE SPACE / Software ordinal: 1
NMR representativeSelection criteria: average structure
NMR ensembleConformers submitted total number: 1

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