As part of structural investigations of components of the molecular motor, dynein, we prepared the light chain, Robl1_mouse, with and without an N-terminal His-tag. We found that the His-tag introduced a spurious binding site for a second protein, IC74. We propose a molecular mechanism for functional interference by the His-tag.
Keywords: Affinity tag, docking, dynein, NMR spectroscopy, protein dynamics, protein-protein interactions
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