1IFR

Structure of Lamin A/C Globular Domain

Summary for 1IFR

• Entry DOI: 10.2210/pdb1ifr/pdb
• Descriptor: Lamin A/C, GLYCEROL (3 entities in total)
• Functional Keywords: immunoglobulin, immune system
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P02545
• Total number of polymer chains: 1
• Total formula weight: 13478.08

Authors

Dhe-Paganon, S.,Werner, E.D.,Shoelson, S.E. (deposition date: 2001-04-13, release date: 2002-07-17, Last modification date: 2024-02-07)

Primary citation

Dhe-Paganon, S.,Werner, E.D.,Chi, Y.I.,Shoelson, S.E.
Structure of the globular tail of nuclear lamin.
J.Biol.Chem., 277:17381-17384, 2002

PubMed Abstract: The nuclear lamins form a two-dimensional matrix that provides integrity to the cell nucleus and participates in nuclear activities. Mutations in the region of human LMNA encoding the carboxyl-terminal tail Lamin A/C are associated with forms of muscular dystrophy and familial partial lipodystrophy (FPLD). To help discriminate tissue-specific phenotypes, we have solved at 1.4-A resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all beta immunoglobulin-like fold. FPLD-associated mutations cluster within a small surface, whereas muscular dystrophy-associated mutations are distributed throughout the protein core and on its surface. These findings distinguish myopathy- and lipodystrophy-associated mutations and provide a structural framework for further testing hypotheses concerning lamin function.

PubMed: 11901143
DOI: 10.1074/jbc.C200038200

Experimental method

X-RAY DIFFRACTION (1.4 Å)