› 1ivt

Solution NMR

NMR structures of the C-terminal globular domain of human lamin A/C

Released:
DOI: 10.2210/pdb1ivt/pdb
PDB entry 1ivt coloured by chain, ensemble of 15 models, front view.
PDB entry 1ivt coloured by chain, ensemble of 15 models, side view.
PDB entry 1ivt coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy.
Krimm I, Ostlund C, Gilquin B, Couprie J, Hossenlopp P, Mornon JP, Bonne G, Courvalin JC, Worman HJ, Zinn-Justin S
Structure 10 811-23 (2002)
PMID: 12057196

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135892 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lamin-A/C Chain: A
Molecule details ›
Chain: A
Length: 122 amino acids
Theoretical weight: 13.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02545 (Residues: 428-549; Coverage: 18%)
Gene names: LMN1, LMNA
Sequence domains: Lamin Tail Domain
Structure domains: Lamin Tail domain

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

Quick links

Citations

72 review citations

Nuclear lamins: major factors in the structural organization and function of the nucleus and chromatin.
Dechat et al. (2008)
71 more

17 mentions without citation

Myopathic lamin mutations cause reductive stress and activate the nrf2/keap-1 pathway.
Dialynas et al. (2015)
16 more