› 2lug

Solution NMR

Solution NMR structure of a S72-S107 peptide of 18.5kDa murine myelin basic protein (MBP) in association with dodecylphosphocholine micelles

Released:
DOI: 10.2210/pdb2lug/pdb
PDB entry 2lug coloured by chain, ensemble of 10 models, front view.
PDB entry 2lug coloured by chain, ensemble of 10 models, side view.
PDB entry 2lug coloured by chain, ensemble of 10 models, top view.
Source organism: Mus musculus
Primary publication:
Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles.
Ahmed MA, De Avila M, Polverini E, Bessonov K, Bamm VV, Harauz G
Biochemistry 51 7475-87 (2012)
PMID: 22947219

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Myelin basic protein Chain: A
Molecule details ›
Chain: A
Length: 36 amino acids
Theoretical weight: 3.98 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04370 (Residues: 206-237; Coverage: 13%)
Gene names: Mbp, Shi
Sequence domains: Myelin basic protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 76%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Myelin management by the 18.5-kDa and 21.5-kDa classic myelin basic protein isoforms.
Harauz et al. (2013)
3 more

4 mentions without citation

The effects of threonine phosphorylation on the stability and dynamics of the central molecular switch region of 18.5-kDa myelin basic protein.
Vassall et al. (2013)
3 more