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'''Structure of Lamin A/C Globular Domain''' | '''Structure of Lamin A/C Globular Domain''' | ||
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[[Category: Shoelson, S E.]] | [[Category: Shoelson, S E.]] | ||
[[Category: Werner, E D.]] | [[Category: Werner, E D.]] | ||
[[Category: | [[Category: Immunoglobulin]] | ||
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Revision as of 16:57, 2 May 2008
Structure of Lamin A/C Globular Domain
Overview
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.
About this Structure
1IFR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the globular tail of nuclear lamin., Dhe-Paganon S, Werner ED, Chi YI, Shoelson SE, J Biol Chem. 2002 May 17;277(20):17381-4. Epub 2002 Mar 18. PMID:11901143 Page seeded by OCA on Fri May 2 19:57:02 2008
