› 8e20

Electron Microscopy
3.6Å resolution

Cryo-EM structure of the full-length human NF1 dimer

Released:
DOI: 10.2210/pdb8e20/pdb
PDB entry 8e20 coloured by chain, front view.
PDB entry 8e20 coloured by chain, side view.
PDB entry 8e20 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Destabilizing NF1 variants act in a dominant negative manner through neurofibromin dimerization.
Young LC, Goldstein de Salazar R, Han SW, Huang ZYS, Merk A, Drew M, Darling J, Wall V, Grisshammer R, Cheng A, Allison MR, Sale MJ, Nissley DV, Esposito D, Ognjenovic J, McCormick F
OpenAccess logo Proc Natl Acad Sci U S A 120 e2208960120 (2023)
PMID: 36689660
Related structures: EMD-27826

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neurofibromin Chains: A, B
Molecule details ›
Chains: A, B
Length: 2818 amino acids
Theoretical weight: 317.41 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P21359 (Residues: 1-2839; Coverage: 99%)
  • Best match: P21359-2 (Residues: 1-2818)
Gene name: NF1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.6Å
Relevant EMDB volumes: EMD-27826
Expression system: Spodoptera frugiperda

Quick links

Citations

2 review citations

Neurofibromatosis Type 1-Associated Optic Pathway Gliomas: Current Challenges and Future Prospects.
Tang et al. (2023)
1 more

1 mention without citation

Destabilizing NF1 variants act in a dominant negative manner through neurofibromin dimerization.
Young et al. (2023)