› 6rmh

Electron Microscopy
9.6Å resolution

The Rigid-body refined model of the normal Huntingtin.

Released:
DOI: 10.2210/pdb6rmh/pdb
PDB entry 6rmh coloured by chain, front view.
PDB entry 6rmh coloured by chain, side view.
PDB entry 6rmh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The Polyglutamine Expansion at the N-Terminal of Huntingtin Protein Modulates the Dynamic Configuration and Phosphorylation of the C-Terminal HEAT Domain.
Jung T, Shin B, Tamo G, Kim H, Vijayvargia R, Leitner A, Marcaida MJ, Astorga-Wells J, Jung R, Aebersold R, Peraro MD, Hebert H, Seong IS, Song JJ
Structure 28 1035-1050.e8 (2020)
PMID: 32668197
Related structures: EMD-4937

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154897 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Huntingtin Chain: A
Molecule details ›
Chain: A
Length: 3142 amino acids
Theoretical weight: 347.97 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P42858 (Residues: 1-3142; Coverage: 100%)
Gene names: HD, HTT, IT15
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 9.6Å
Relevant EMDB volumes: EMD-4937
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Deciphering the Structure and Formation of Amyloids in Neurodegenerative Diseases With Chemical Biology Tools.
Landrieu et al. (2022)
3 more

2 mentions without citation

Big versus small: The impact of aggregate size in disease.
Hnath et al. (2023)
1 more