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ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins

Ponting, Chris P., Blake, Derek J., Davies, Kay E., Kendrick-Jones, John and Winder, Steven J. 1996. ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins. Trends in Biochemical Sciences 21 (1) , pp. 11-13. 10.1016/S0968-0004(06)80020-4

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Duchenne muscular dystrophy (DMD) is a severe, X-chromosome-linked musclewasting disease that affects approximately one in 3500 male births and is caused by a lack of the protein dystrophin. Dystrophin is a 427 kDa protein comprising five main regions, which are, from the amino terminus: an F-actinbinding domain (homologous to regions of alpha-actinin and beta-spectrin), a rod-like coiled-coilregion containing 24 spectrin-like repeats, a WW domain, a cysteine-rich region and a carboxy-terminal coiled-coil domain. In-frame deletions within either the actin-binding or the rod-like domains in the DMD gene result in a range of Becker muscular dystrophy (BMD) phenotypes ranging from mild to relatively severe, suggesting that these regions are important, but are not absolute requirements for molecular function. By contrast, mutations within the cysteine-rich region and the first half of the carboxy-terminal domain almost invariably result in the severe DMD phenotypes.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
MRC Centre for Neuropsychiatric Genetics and Genomics (CNGG)
Subjects: R Medicine > R Medicine (General)
Publisher: Elsevier
ISSN: 0968-0004
Last Modified: 04 Jun 2017 05:12

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