Journal article

Two-dimensional electrophoretic analysis of mixed lineage kinase 2 N-terminal domain binding proteins

RK Rasmussen, H Ji, JS Eddes, RL Moritz, GE Reid, RJ Simpson, DS Dorow

ELECTROPHORESIS | WILEY-V C H VERLAG GMBH | Published : 1998

Abstract

The mixed lineage kinase 2 (MLK2) protein contains several structurally distinct domains including an src homology (SH) 3 domain, a kinase catalytic domain, two leucine zippers, a basic motif and a cdc42/rac interactive binding motif. These domains have been recognized mainly for their involvement in protein-protein interactions in signal transduction networks. The SH3 domain in particular has been implicated in control of signaling events. To identify proteins that interact with MLK2, the N-terminal 100 amino acids, including the SH3 domain, were expressed as a glutathione S-transferase (GST) fusion protein. This fusion protein (MLK2N) was used as an affinity ligand to isolate binding prote..

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University of Melbourne Researchers