The solution structure of the leucine zipper motif of the Jun oncoprotein homodimer

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Abstract
Proton NMR studies have been performed on a 9.8‐kDa synthetic fragment comprising the homodimeric leucine zipper domain of the human oncoprotein Jun to ascertain its conformation in aqueous solution. Analysis of two‐dimensional scalar and dipolar‐coupling experiments enabled almost all proton resonances to be sequence‐specifically assigned and further revealed that the Jun leucine zipper forms a completely symmetric dimer in solution, consistent with the formation of a coiled‐coil arrangement of parallel α‐helical strands. The rates of exchange of individual amide protons with solvent, as well as hydrogen‐bond lengths predicted from amide proton chemical shifts, are shown to correlate with residue position in the coiled‐coil. A subset of 209 unambiguous distance constraints was compiled using rules recently formulated for interpreting the NOESY spectra of symmetric coiled‐coils, and these were used in combination with experimentally determined hydrogen bond and dihedral angle constraints to compute a solution structure for the Jun leucine zipper domain.

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