The solution structure of a leucine-zipper motif peptide.
We report the complete structure determination of a 34 residue synthetic peptide with the amino acid sequence of the dimerization domain (leucine zipper) of GCN4. A high resolution structure in solution was obtained by 1H-NMR studies and distance geometry calculations followed by restrained energy minimization. A set of 20 final structures was obtained with an average root mean square deviation of 1.3 A for the backbone atoms (excluding the first and the last two residues). The structure contains an uninterrupted helix. A comparison with a structure previously determined for a larger peptide containing both the DNA-binding region (basic region) and the leucine-zipper motif shows the structural independence of the leucine-zipper domain from the contiguous DNA binding region.
Saudek
V
V
Marion Merrell Dow Research Institute, Strasbourg, France.
Pastore
A
A
Morelli
M A
MA
Frank
R
R
Gausepohl
H
H
Gibson
T
T
D000595:Amino Acid Sequence; D004268:DNA-Binding Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D005656:Fungal Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D016350:Leucine Zippers; D009682:Magnetic Resonance Spectroscopy; D008433:Mathematics; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D011494:Protein Kinases; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions; D014157:Transcription Factors / Q000138:chemical synthesis / Q000737:chemistry*
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; D012996:Solutions; D014157:Transcription Factors; D011494:Protein Kinases