Journal article

Mechanism of oligomerisation of cyclase-associated protein from Dictyostelium discoideum in solution.

Adlina Mohd Yusof, Elmar Jaenicke, Jan Skov Pedersen, Angelika A Noegel, Michael Schleicher, Andreas Hofmann

Journal of Molecular Biology | Published : 2006

Abstract

Cyclase-associated protein (CAP) is a highly conserved modular protein implicated in the regulation of actin filament dynamics and a variety of developmental and morphological processes. The protein exists as a high molecular weight complex in cell extracts and purified protein possesses a high tendency to aggregate, a major obstacle for crystallisation. Using a mutagenesis approach, we show that two structural features underlie the mechanism of oligomerisation in Dictyostelium discoideum CAP. Positively charged clusters on the surface of the N-terminal helix-barrel domain are involved in inter-molecular interactions with the N or C-terminal domains. Abolishing these interactions mainly rend..

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University of Melbourne Researchers