Structure of the globular tail of nuclear lamin. J Biol Chem 2002 May 17;277(20):17381-4
Date
03/20/2002Pubmed ID
11901143DOI
10.1074/jbc.C200038200Scopus ID
2-s2.0-0037124053 (requires institutional sign-in at Scopus site) 236 CitationsAbstract
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.
Author List
Dhe-Paganon S, Werner ED, Chi YI, Shoelson SEAuthor
Young-In Chi PhD Assistant Professor in the Data Science Institute department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Annelida
Anura
Crystallography, X-Ray
Diptera
Fishes
Humans
Lamin Type A
Lamins
Lipodystrophy
Models, Molecular
Molecular Sequence Data
Muscular Dystrophies
Nuclear Proteins
Protein Conformation
Sequence Homology, Amino Acid
