1IVT: NMR structures of the C-terminal globular domain of human lamin A/C

Citation:
Abstract
Lamins are nuclear intermediate filaments that, together with lamin-associated proteins, maintain nuclear shape and provide a structural support for chromosomes and replicating DNA. We have determined the solution structure of the human lamin A/C C-terminal globular domain which contains specific mutations causing four different heritable diseases. This domain encompasses residues 430-545 and adopts an Ig-like fold of type s. We have also characterized by NMR and circular dichroism the structure and thermostability of three mutants, R453W and R482W/Q, corresponding to "hot spots" causing Emery-Dreifuss muscular dystrophy and Dunnigan-type lipodystrophy, respectively. Our structure determination and mutant analyses clearly show that the consequences of the mutations causing muscle-specific diseases or lipodystrophy are different at the molecular level.
PDB ID: 1IVTDownload
MMDB ID: 20373
PDB Deposition Date: 2002/3/29
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 1IVT
Label Count Molecule
Protein (1 molecule)
1
Lamin A/C(Gene symbol: LMNA)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
.