3GEF

Crystal structure of the R482W mutant of lamin A/C

3GEF の概要

• エントリーDOI: 10.2210/pdb3gef/pdb
• 分子名称: Lamin-A/C (2 entities in total)
• 機能のキーワード: immunoglobulin fold, lamin, cardiomyopathy, charcot-marie-tooth disease, disease mutation, intermediate filament, limb-girdle muscular dystrophy, lipoprotein, nucleus, phosphoprotein, prenylation, structural protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus. Isoform C: Nucleus speckle : P02545
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 52378.45

構造登録者

Magracheva, E.,Kozlov, S.,Stuart, C.,Wlodawer, A.,Zdanov, A. (登録日: 2009-02-25, 公開日: 2009-08-04, 最終更新日: 2024-11-27)

主引用文献

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

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: 19574635
DOI: 10.1107/S1744309109020302

実験手法

X-RAY DIFFRACTION (1.5 Å)