Skip NavigationSkip to Content
Return Return to Search Results

Structure of the lamin A/C R482W mutant responsible for dominant familial partial lipodystrophy (FPLD)

  1. Author:
    Magracheva, E.
    Kozlov, S.
    Stewart, C. L.
    Wlodawer, A.
    Zdanov, A.

  2. Author Address

    Magracheva, Eugenia, Zdanov, Alexander] NCI, Basic Res Program SAIC Frederick, Frederick, MD 21702 USA. [Kozlov, Serguei, Stewart, Colin L.] NCI, Canc & Dev Biol Lab, Frederick, MD 21702 USA. [Wlodawer, Alexander] NCI, Macromol Crystallog Lab, Frederick, MD 21702 USA.
    1. Year: 2009
  2. Journal: Acta Crystallographica Section F-Structural Biology and Crystallization Communications
    1. 65
    2. Pages: 665-670
  4. Type of Article: Article
  1. 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 angstrom 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.

    See More

  1. Keywords:

External Sources

  1. View Full Text
  2. DOI: 10.1107/s1744309109020302
  3. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel