Toggle Main Menu Toggle Search

Open Access padlockePrints

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


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


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


DOI: 10.1016/j.jmb.2008.04.046

PubMed id: 18495154


Altmetrics provided by Altmetric


Funder referenceFunder name
Biotechnology and Biological Sciences Research Council
G0601943Medical Research Council
MC_U117533887Medical Research Council
MC_U117574559Medical Research Council