› 1lg4

Solution NMR

NMR structure of the human doppel protein fragment 24-152

Released:
DOI: 10.2210/pdb1lg4/pdb
PDB entry 1lg4 coloured by chain, ensemble of 20 models, front view.
PDB entry 1lg4 coloured by chain, ensemble of 20 models, side view.
PDB entry 1lg4 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
NMR structure of the human doppel protein.
Lührs T, Riek R, Güntert P, Wüthrich K
J Mol Biol 326 1549-57 (2003)
PMID: 12595265

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Prion-like protein doppel Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9UKY0 (Residues: 24-152; Coverage: 84%)
Gene names: DPL, PRND, UNQ1830/PRO3443
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Mammalian prion biology: one century of evolving concepts.
Aguzzi et al. (2004)
6 more

12 mentions without citation

Developmental and pathogenic mechanisms of basement membrane assembly.
Yurchenco et al. (2009)
11 more