Towards a complete atomic structure of spectrin family proteins

Broderick, M.J.F. and Winder, S.J. (2002) Towards a complete atomic structure of spectrin family proteins. Journal of Structural Biology, 137, pp. 184-193. (doi: 10.1006/jsbi.2002.4465)

Full text not currently available from Enlighten.


The spectrin family of proteins represents a discrete group of cytoskeletal proteins comprising principally α-actinin, spectrin, dystrophin, and homologues and isoforms. They all share three main structural and functional motifs, namely, the spectrin repeat, EF-hands, and a CH domain-containing actin-binding domain. These proteins are variously involved in organisation of the actin cytoskeleton, membrane cytoskeleton architecture, cell adhesion, and contractile apparatus. The highly modular nature of these molecules has been a hindrance to the determination of their complete structures due to the inherent flexibility imparted on the proteins, but has also been an asset, inasmuch as the individual modules were of a size amenable to structural analysis by both crystallographic and NMR approaches. Representative structures of all the major domains shared by spectrin family proteins have now been solved at atomic resolution, including in some cases multiple domains from several family members. High-resolution structures, coupled with lower resolution methods to determine the overall molecular shape of these proteins, allow us for the first time to build complete atomic structures of the spectrin family of proteins.

Item Type:Articles
Glasgow Author(s) Enlighten ID:UNSPECIFIED
Authors: Broderick, M.J.F., and Winder, S.J.
College/School:College of Medical Veterinary and Life Sciences
Journal Name:Journal of Structural Biology

University Staff: Request a correction | Enlighten Editors: Update this record