ePrints

Solution Structure of the Inner DysF Domain of Myoferlin and Implications for Limb Girdle Muscular Dystrophy Type 2B

Lookup NU author(s): Dr Eugen-Matthias Strehle, Emerita Professor Katherine Bushby

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

Mutations in the protein dysferlin, a member of the ferlin family, lead to limb girdle muscular dystrophy type 2B and Myoshi myopathy. The ferlins are large proteins characterised by multiple C2 domains and a single C-terminal membrane-spanning helix. However, there is sequence conservation in some of the ferlin family in regions outside the C2 domains. In one annotation of the domain structure of these proteins, an unusual internal duplication event has been noted where a putative domain is inserted in between the N- and C-terminal parts of a homologous domain. This domain is known as the DysF domain. Here, we present the solution structure of the inner DysF domain of the dysferlin paralogue myoferlin, which has a unique fold held together by stacking of arginine and tryptophans, mutations that lead to clinical disease in dysferlin. © 2008 Elsevier Ltd. All rights reserved.

Publication metadata

Author(s): Patel P, Harris R, Geddes SM, Strehle E-M, Watson JD, Bashir R, Bushby K, Driscoll PC, Keep NH

Publication type: Article

Publication status: Published

Journal: Journal of Molecular Biology

Year: 2008

Volume: 379

Issue: 5

Pages: 981-990

Print publication date: 20/06/2008

ISSN (print): 0022-2836

ISSN (electronic): 1089-8638

Publisher: Academic Press

URL: http://dx.doi.org/10.1016/j.jmb.2008.04.046

DOI: 10.1016/j.jmb.2008.04.046

PubMed id: 18495154

Altmetrics

Funding

Share