Structure of the globular tail of nuclear lamin

Sirano Dhe-Paganon, Eric D. Werner, Young In Chi, Steven E. Shoelson

Research output: Contribution to journalArticlepeer-review

197 Scopus citations

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-Å resolution the three-dimensional crystal structure of the lamin A/C globular tail. The domain adopts a novel, all β 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.

Original languageEnglish (US)
Pages (from-to)17381-17384
Number of pages4
JournalJournal of Biological Chemistry
Volume277
Issue number20
DOIs
StatePublished - May 17 2002

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