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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Bollati M,Barbiroli A,Favalli V,Arbustini E,Charron P,Bolognesi M

doi

10.1016/j.bbrc.2011.12.136

subject

Has Abstract

pub_date

2012-02-10 00:00:00

pages

217-21

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(11)02345-X

journal_volume

418

pub_type

杂志文章

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