Leucine Zippers
نویسنده
چکیده
The leucine zipper (ZIP) motif consists of a periodic repetition of a leucine residue at every seventh position and forms an a-helical conformation, which facilitates dimerization and in some cases higher oligomerization of proteins. Inmany eukaryotic gene regulatory proteins, the ZIP motif is flanked at its N-terminus by a basic region containing characteristic residues that facilitate DNA binding.
منابع مشابه
Predicting leucine zipper structures from sequence.
The leucine zipper structure is adopted by one family of the coiled coil proteins. Leucine zippers have a characteristic leucine repeat: Leu-X6-Leu-X6-Leu-X6-Liu (where X may be any residue). However, many sequences have the leucine repeat, but do not adopt the leucine zipper structure (we shall refer to these as non-zippers). We have found and analyzed residue pair patterns that allow one to i...
متن کاملThermodynamic analysis of the heterodimerization of leucine zippers of Jun and Fos transcription factors.
Jun and Fos are components of the AP1 family of transcription factors and bind to the promoters of a diverse multitude of genes involved in critical cellular responses such as cell growth and proliferation, cell cycle regulation, embryonic development and cancer. Here, using the powerful technique of isothermal titration calorimetry, we characterize the thermodynamics of heterodimerization of l...
متن کاملHelical supramolecules and fibers utilizing leucine zipper-displaying dendrimers.
We describe a new family of discrete supramolecules comprising leucine-zipper peptides noncovalently assembled upon cognate leucine zippers fused to a dendrimer core. Circular dichroism and sedimentation equilibrium experiments clearly demonstrate that each leucine-zipper dendrimer (D-EZ4 or D-KZ4) can noncovalently display four leucine zippers on their surface that can be utilized for the mult...
متن کاملPreferential heterodimer formation by isolated leucine zippers from fos and jun.
The products of the nuclear oncogenes fos and jun are known to form heterodimers that bind to DNA and modulate transcription. Both proteins contain a leucine zipper that is important for heterodimer formation. Peptides corresponding to these leucine zippers were synthesized. When mixed, these peptides preferentially form heterodimers over homodimers by at least 1000-fold. Both homodimers and th...
متن کاملComputational approaches to identify Leucine Zippers
The leucine zipper is a dimerization domain occurring mostly in regulatory and thus in many oncogenic proteins. The leucine repeat in the sequence has been traditionally used for identification, however with poor reliability. The coiled coil structure of a leucine zipper is required for dimerization and can be predicted with reasonable accuracy by existing algorithms. We exploit this fact for i...
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تاریخ انتشار 2005