Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 277, Issue 20, Pages 17381-17384Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C200038200
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Funding
- NIDDK NIH HHS [R01 DK43123, DK09393] Funding Source: Medline
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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-Angstrom resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all beta-mmunoglobulin-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.
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