Structures of the lamin A/C R335W and E347K mutants: Implications for dilated cardiolaminopathies

Michela Bollati, Alberto Barbiroli, Valentina Favalli, Eloisa Arbustini, Philippe Charron, Martino Bolognesi

Research output: Contribution to journalArticlepeer-review

Abstract

Dilated cardiomyopathy (DCM) is a condition whereby the normal muscular function of the myocardium is altered by specific or multiple aetiologies. About 25-35% of DCM patients show familial forms of the disease, with most mutations affecting genes encoding cytoskeletal proteins. Most of the DCM-related mutations fall in the Lamin AC gene, in particular in the Coil2B domain of the encoded protein. In this context, we focussed our studies on the crystal structures of two lamin Coil2B domain mutants (R335W and E347K). Both R335 and E347 are higly conserved residues whose substitution has little effects on the Coil2B domain three-dimensional structure; we can thus hypothesize that the mutations may interfere with the binding of components within the nuclear lamina, or of nuclear factors, that have been proposed to interact/associate with lamin A/C.

Original languageEnglish
Pages (from-to)217-221
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume418
Issue number2
DOIs
Publication statusPublished - Feb 10 2012

Keywords

  • Coiled coil
  • Crystal structure
  • Dilated cardiomyopathy
  • Laminopathy
  • Nuclear lamins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

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