The solution structure of the leucine zipper motif of the Jun oncoprotein homodimer.
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 alpha-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.
Department of Biochemistry, University of Sydney, Australia.
F K
FK
Junius
A S
AS
Weiss
G F
GF
King
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D006860:Hydrogen Bonding; D016350:Leucine Zippers; D046911:Macromolecular Substances; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016755:Proto-Oncogene Proteins c-jun / Q000737:chemistry*; D012996:Solutions
D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D016755:Proto-Oncogene Proteins c-jun; D012996:Solutions