Volume 9 Issue 8, August 2002

Desmoplakin is a major and essential constituent of the interface between the transmembrane glycoproteins mediating adhesion and the intermediate filament cytoskeleton in the cell interior. The structures of two desmoplakin domains that participate in intermediate filament binding reveal that a unique 38-amino acid repeat-containing domain shared with related proteins packs in a novel globular fold.

CheZ is a protein involved in signal transduction in bacterial chemotaxis and accelerates the dephosphorylation of the activated response regulator, CheY-phosphate. The crystal structure of CheZ in complex with activated CheY provides insights into the function of CheZ.

An example of crosstalk between 'tails' of different histones within nucleosomes suggests novel mechanisms of chromatin regulation.

NMR spectra recorded on the 900 kDa GroEL–GroES complex substantially raise the bar for the size of macromolecules that can be studied by NMR techniques.