Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

The contraction-relaxation cycle of muscle cells translates into large movements of several filament systems in sarcomeres, requiring special molecular mechanisms to maintain their structural integrity. Recent structural and functional data from three filaments harboring extensive arrays of immunoglobulin-like domains - titin, filamin and myomesin--have, for the first time, unraveled a common function of their terminal domains: assembly and anchoring of the respective filaments. In each case, the protein-protein interactions are mediated by antiparallel dimerization modules via intermolecular beta-sheets. These observations on terminal filament assembly indicate an attractive model for several other filament proteins that require structural characterization.

Original publication

DOI

10.1016/j.tibs.2008.09.009

Type

Journal article

Journal

Trends biochem sci

Publication Date

01/2009

Volume

34

Pages

33 - 39

Keywords

Animals, Biochemistry, Connectin, Contractile Proteins, Filamins, Humans, Immunoglobulins, Microfilament Proteins, Microscopy, Electron, Muscle Proteins, Myosins, Protein Binding, Protein Interaction Mapping, Protein Kinases, Protein Structure, Secondary, Protein Structure, Tertiary, Sarcomeres