3GEF
Crystal structure of the R482W mutant of lamin A/C
Summary for 3GEF
Entry DOI | 10.2210/pdb3gef/pdb |
Descriptor | Lamin-A/C (2 entities in total) |
Functional Keywords | immunoglobulin fold, lamin, cardiomyopathy, charcot-marie-tooth disease, disease mutation, intermediate filament, limb-girdle muscular dystrophy, lipoprotein, nucleus, phosphoprotein, prenylation, structural protein |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus. Isoform C: Nucleus speckle : P02545 |
Total number of polymer chains | 4 |
Total formula weight | 52378.45 |
Authors | Magracheva, E.,Kozlov, S.,Stuart, C.,Wlodawer, A.,Zdanov, A. (deposition date: 2009-02-25, release date: 2009-08-04, Last modification date: 2024-11-27) |
Primary citation | Magracheva, E.,Kozlov, S.,Stewart, C.L.,Wlodawer, A.,Zdanov, A. Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD). Acta Crystallogr.,Sect.F, 65:665-670, 2009 Cited by PubMed Abstract: Proteins of the A-type lamin family, which consists of two members, lamin A and lamin C, are the major components of a thin proteinaceous filamentous meshwork, the lamina, that underlies the inner nuclear membrane. A-type lamins have recently become the focus of extensive functional studies as a consequence of the linking of at least eight congenital diseases to mutations in the lamin A/C gene (LMNA). This spectrum of pathologies, which mostly manifest themselves as dominant traits, includes muscle dystrophies, dilated cardiomyopathies, the premature aging syndrome Hutchinson-Guilford progeria and familial partial lipodystrophy (FPLD). The crystal structure of the lamin A/C mutant R482W, a variant that causes FPLD, has been determined at 1.5 A resolution. A completely novel aggregation state of the C-terminal globular domain and the position of the mutated amino-acid residue suggest means by which the mutation may affect lamin A/C-protein and protein-DNA interactions. PubMed: 19574635DOI: 10.1107/S1744309109020302 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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