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J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18.

Structure of the globular tail of nuclear lamin.

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  • 1Joslin Diabetes Center & Department of Medicine, Harvard Medical School, Boston, Massachusetts 02215, USA.

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.

PMID:
11901143
[PubMed - indexed for MEDLINE]
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