› 1cek

Solid-state NMR

THREE-DIMENSIONAL STRUCTURE OF THE MEMBRANE-EMBEDDED M2 CHANNEL-LINING SEGMENT FROM THE NICOTINIC ACETYLCHOLINE RECEPTOR BY SOLID-STATE NMR SPECTROSCOPY

Released:
DOI: 10.2210/pdb1cek/pdb
PDB entry 1cek coloured by chain, front view.
PDB entry 1cek coloured by chain, side view.
PDB entry 1cek coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy.
Opella SJ, Marassi FM, Gesell JJ, Valente AP, Kim Y, Oblatt-Montal M, Montal M
Nat Struct Biol 6 374-9 (1999)
PMID: 10201407

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150387 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholine receptor subunit delta Chain: A
Molecule details ›
Chain: A
Length: 25 amino acids
Theoretical weight: 2.67 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P25110 (Residues: 276-298; Coverage: 5%)
Gene names: Acrd, Chrnd

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: ORIENTATIONAL CONSTRAINTS
Expression system: Escherichia coli BL21

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Citations

45 review citations

Nicotinic receptors at the amino acid level.
Corringer et al. (2000)
44 more

8 mentions without citation

Membrane protein structure from rotational diffusion.
Das et al. (2015)
7 more