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- PDB-2csa: Structure of the M3 Muscarinic Acetylcholine Receptor Basolateral... -

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Basic information

Entry
Database: PDB / ID: 2csa
TitleStructure of the M3 Muscarinic Acetylcholine Receptor Basolateral Sorting Signal
ComponentsMuscarinic acetylcholine receptor M3
KeywordsSignaling Protein/MEMBRANE PROTEIN / BASOLATERAL SORTING-SIGNAL BLSS BETA-TURN / Signaling Protein-MEMBRANE PROTEIN COMPLEX
Function / homology
Function and homology information


regulation of monoatomic ion transmembrane transporter activity / regulation of vascular associated smooth muscle contraction / saliva secretion / ion channel modulating, G protein-coupled receptor signaling pathway / Acetylcholine regulates insulin secretion / Muscarinic acetylcholine receptors / phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / G protein-coupled acetylcholine receptor activity / adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway / positive regulation of smooth muscle contraction ...regulation of monoatomic ion transmembrane transporter activity / regulation of vascular associated smooth muscle contraction / saliva secretion / ion channel modulating, G protein-coupled receptor signaling pathway / Acetylcholine regulates insulin secretion / Muscarinic acetylcholine receptors / phospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway / G protein-coupled acetylcholine receptor activity / adenylate cyclase-inhibiting G protein-coupled acetylcholine receptor signaling pathway / positive regulation of smooth muscle contraction / phosphatidylinositol phospholipase C activity / G protein-coupled serotonin receptor activity / acetylcholine binding / acetylcholine receptor signaling pathway / ligand-gated ion channel signaling pathway / G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger / smooth muscle contraction / basal plasma membrane / calcium-mediated signaling / protein modification process / G protein-coupled acetylcholine receptor signaling pathway / positive regulation of insulin secretion / signaling receptor activity / nervous system development / G alpha (q) signalling events / chemical synaptic transmission / basolateral plasma membrane / postsynaptic membrane / G protein-coupled receptor signaling pathway / synapse / dendrite / endoplasmic reticulum membrane / signal transduction / plasma membrane
Similarity search - Function
Muscarinic acetylcholine receptor M3 / Muscarinic acetylcholine receptor 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
Muscarinic acetylcholine receptor M3
Similarity search - Component
MethodSOLUTION NMR / Distance Geometry, Simulated Annealing, Energy minimization
AuthorsIverson, H.A. / Fox, D. / Nadler, L.S. / Klevit, R.E. / Nathanson, N.M.
CitationJournal: J.Biol.Chem. / Year: 2005
Title: Identification and structural determination of the M3 muscarinic acetylcholine receptor basolateral sorting signal.
Authors: Iverson, H.A. / Fox, D. / Nadler, L.S. / Klevit, R.E. / Nathanson, N.M.
History
DepositionMay 21, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 31, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Muscarinic acetylcholine receptor M3


Theoretical massNumber of molelcules
Total (without water)1,9951
Polymers1,9951
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)10 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Muscarinic acetylcholine receptor M3 /


Mass: 1995.024 Da / Num. of mol.: 1 / Fragment: THIRD INTRACELLULAR LOOP (Residues:271-289) / Source method: obtained synthetically
Details: The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human).
References: UniProt: P20309

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D TOCSY
1222D TOCSY
1312D NOESY
2412D NOESY
3512D NOESY
4612D NOESY
5712D NOESY
6812D NOESY
191DQF-COSY
NMR detailsText: NOESY spectra were collected with a mixing time of 300ms

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Sample preparation

Details
Solution-IDContentsSolvent system
11-2mM M3 peptide, unlabeled, 50mM sodium phosphate buffer, 1mM EDTA, 1mM NaN3, 90% H2O, 10% D2090% H2O, 10% D20
21-2mM M3 peptide, unlabeled, 50mM sodium phosphate buffer, 1mM EDTA, 1mM NaN3, 99.9 % D20, 0.1% H2099.9 % D20, 0.1% H20
Sample conditions
Conditions-IDpHPressure (kPa)Temperature (K)
16.4 ambient 285 K
26.4 ambient 278 K
36.4 ambient 288 K
46.4 ambient 298 K
56.4 ambient 308 K
66.4 ambient 318 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 500 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Brukercollection
NMRPipeDelaglioprocessing
NMRView5Delagliodata analysis
CNS1.1Brungerrefinement
RefinementMethod: Distance Geometry, Simulated Annealing, Energy minimization
Software ordinal: 1
Details: Structures are based on a total of 58 inter-residue NOE distance restraints and 5 dihedral angle restraints
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 10

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