1IVT

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

Summary for 1IVT

• Entry DOI: 10.2210/pdb1ivt/pdb
• Descriptor: Lamin A/C (1 entity in total)
• Functional Keywords: beta barrel, all sheet, ig-fold, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P02545
• Total number of polymer chains: 1
• Total formula weight: 13506.14

Authors

Krimm, I.,Ostlund, C.,Gilquin, B.,Couprie, J.,Hossenlopp, P.,Mornon, J.P.,Bonn, G.,Courvalin, J.C.,Worman, H.J.,Zinn-Justin, S. (deposition date: 2002-03-29, release date: 2002-08-21, Last modification date: 2023-12-27)

Primary citation

Krimm, I.,Ostlund, C.,Gilquin, B.,Couprie, J.,Hossenlopp, P.,Mornon, J.P.,Bonne, G.,Courvalin, J.C.,Worman, H.J.,Zinn-Justin, S.
The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy.
Structure, 10:811-823, 2002

PubMed 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.

PubMed: 12057196
DOI: 10.1016/S0969-2126(02)00777-3

Experimental method

SOLUTION NMR