› 1mot

Solution NMR

NMR Structure Of Extended Second Transmembrane Domain Of Glycine Receptor alpha1 Subunit in SDS Micelles

Released:
DOI: 10.2210/pdb1mot/pdb
PDB entry 1mot coloured by chain, ensemble of 20 models, front view.
PDB entry 1mot coloured by chain, ensemble of 20 models, side view.
PDB entry 1mot coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure and backbone dynamics of the extended second transmembrane domain of the human neuronal glycine receptor alpha1 subunit.
Yushmanov VE, Mandal PK, Liu Z, Tang P, Xu Y
Biochemistry 42 3989-95 (2003)
PMID: 12667090

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149955 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine receptor subunit alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 28 amino acids
Theoretical weight: 2.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P23415 (Residues: 277-304; Coverage: 7%)
Gene name: GLRA1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Alpha-helical transmembrane peptides: a "divide and conquer" approach to membrane proteins.
Bordag et al. (2010)
3 more

3 mentions without citation

New hyperekplexia mutations provide insight into glycine receptor assembly, trafficking, and activation mechanisms.
Bode et al. (2013)
2 more