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- PDB-1cek: THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-L... -

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Basic information

Entry
Database: PDB / ID: 1cek
TitleTHREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY
ComponentsPROTEIN (ACETYLCHOLINE RECEPTOR M2)
KeywordsACETYLCHOLINE RECEPTOR / M2 / LIPID BILAYERS / ION-CHANNEL
Function / homology
Function and homology information


Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / postsynaptic specialization membrane / acetylcholine binding / ligand-gated monoatomic ion channel activity / monoatomic cation transport / skeletal muscle contraction ...Highly sodium permeable postsynaptic acetylcholine nicotinic receptors / skeletal muscle tissue growth / musculoskeletal movement / acetylcholine-gated channel complex / acetylcholine-gated monoatomic cation-selective channel activity / postsynaptic specialization membrane / acetylcholine binding / ligand-gated monoatomic ion channel activity / monoatomic cation transport / skeletal muscle contraction / regulation of membrane potential / transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential / neuromuscular junction / transmembrane signaling receptor activity / neuron projection / synapse / plasma membrane
Similarity search - Function
Nicotinic acetylcholine receptor / Neurotransmitter-gated ion-channel, conserved site / Neurotransmitter-gated ion-channels signature. / Neurotransmitter-gated ion-channel transmembrane domain / Neurotransmitter-gated ion-channel transmembrane region / Neurotransmitter-gated ion-channel transmembrane domain superfamily / Neuronal acetylcholine receptor / Neurotransmitter-gated ion-channel / Neurotransmitter-gated ion-channel ligand-binding domain / Neurotransmitter-gated ion-channel ligand-binding domain superfamily / Neurotransmitter-gated ion-channel ligand binding domain
Similarity search - Domain/homology
Acetylcholine receptor subunit delta
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodSOLID-STATE NMR / ORIENTATIONAL CONSTRAINTS
AuthorsMarassi, F.M. / Gesell, J.J. / Kim, Y. / Valente, A.P. / Oblatt-Montal, M. / Montal, M. / Opella, S.J.
Citation
Journal: Nat.Struct.Biol. / Year: 1999
Title: Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.
Authors: Opella, S.J. / Marassi, F.M. / Gesell, J.J. / Valente, A.P. / Kim, Y. / Oblatt-Montal, M. / Montal, M.
#1: Journal: To be Published
Title: Dilute Spin-Exchange Assignment of Solid-State NMR Spectra of Oriented Proteins: Acetylcholine Receptor M2 Peptide in Bilayers
Authors: Marassi, F.M. / Gesell, J.J. / Valente, A.P. / Kim, Y. / Oblatt-Montal, M. / Montal, M. / Opella, S.J.
History
DepositionMar 9, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Mar 11, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: 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: PROTEIN (ACETYLCHOLINE RECEPTOR M2)


Theoretical massNumber of molelcules
Total (without water)2,6661
Polymers2,6661
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)1 / 24LOWEST ENERGY
Representative

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Components

#1: Protein/peptide PROTEIN (ACETYLCHOLINE RECEPTOR M2) / ACHR M2


Mass: 2666.143 Da / Num. of mol.: 1 / Fragment: M2 DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Cell: NEURON / Cellular location: POST-SYNAPTIC MEMBRANE / Organ: BRAIN / Plasmid: PGEX FUSION / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P25110

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Experimental details

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Experiment

ExperimentMethod: SOLID-STATE NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N SHIFT/1H-15N DIPOLAR COUPLING PISEMA
12115N SHIFT/15N SHIFT HETCOR
1311H SHIFT/15N SHIFT/1H-15N DIPOLAR COUPLING CORRELATION
NMR detailsText: LOWEST ENERGY. SAMPLE: DMPC BILAYERS ORIENTED ON GLASS SLIDES 15N CHEMICAL SHIFT, 1H CHEMICAL SHIFT AND 1H-15N DIPOLAR COUPLING FREQUENCIES WERE MEASURED FROM PISEMA AND

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Sample preparation

DetailsContents: DMPC
Sample conditionspH: 6.0 / Temperature: 295 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Home-built HOMEBUILTHome-builtHOMEBUILT4001
CHEMAGNETICS CMX400CHEMAGNETICSCMX4005502

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Processing

NMR software
NameClassification
FISIstructure solution
BACKTORstructure solution
RESTRICTstructure solution
RESTRICTrefinement
RefinementMethod: ORIENTATIONAL CONSTRAINTS / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 24 / Conformers submitted total number: 1

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