Article
Nuclear magnetic resonance characterization of the Jun leucine zipper domain: unusual properties of coiled-coil interfacial polar residues.
Biochemistry - 9 May 1995
Junius F K, Mackay J P, Bubb W A, Jensen S A, Weiss A S, King G F
Abstract excerpt
Leucine zippers constitute a widely observed structural motif which serves to promote both homo- and heterodimerization in a number of DNA-binding proteins. As part of our ongoing efforts to characterize both the structure and the dynamical properties of this dimerization domain as they relate to biological function, we report here the secondary structure in solution of a recombinant dimeric peptide (rJunLZ)...
Topics
- Amino Acid Sequence
- Cloning, Molecular
- Genes, jun
- Leucine
- Leucine Zippers
- Magnetic Resonance Spectroscopy
- Models, Chemical
- Molecular Sequence Data
- Mutation
- Protein Structure, Secondary