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Papers In Press, published online ahead of print March 18, 2002
Harvard Medical School, Boston, MA 02215
Corresponding Author: steven.shoelson{at}joslin.harvard.edu
The nuclear lamins form a two-dimensional matrix that provides integrity to the cell nucleus and participates in nuclear activities. Mutations in human Lamin A/C are linked to pathological defects in muscle (Emery-Dreifuss muscular dystrophy, EDMD; dilated cardiomyopathy and conduction system defect, DCM-CD; and limb-girdle muscular dystrophy, LGMD) and adipose tissue (Dunnigan-type familial partial lipodystrophy, FPLD) development. Mutations associated with the muscular dystrophies map throughout the LMNA gene, including regions that encode the amino-terminal helical rod and carboxyl-terminal globular domains. By contrast, mutations associated with FPLD map selectively to the region encoding the globular tail. In order to help discriminate tissue-specific phenotypes, we have solved at 1.4 Å resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all
J. Biol. Chem, 10.1074/jbc.C200038200
Submitted on January 17, 2002
Revised on March 4, 2002
Accepted on March 15, 2002
Structure of the globular tail of nuclear lamin
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.
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