Addition of aos decreases Egfr-spi interaction.

Interaction in vitro; bait and prey produced and purified from transfected constructs.

Interaction in vitro; bait produced as a recombinant fusion protein in S2 cell line; prey produced as a recombinant fusion protein.

Interaction of spi with Egfr is not affected by mutation of the spi palmitoylation site at residue Cys29.

Positive control.

Mutations that compromise dimerization of the Egfr protein (\'s-dEGFR[dim-arm]\') appear to abolish the negative cooperativity observed for this reaction.

Determined binding curves.

Purified protein preps from S2 cells transfected with tagged spi construct and Egfr partial-coding-region construct.

Used extracellular region of the Egfr protein, except domain V; removal of domain V was necessary to allow crystallization of the ligand-receptor complex.