Comprehensive identification of human bZIP interactions with coiled-coil arrays
| Autor: | Amy E. Keating, John R. S. Newman |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Leucine zipper
Protein Folding Protein Array Analysis Computational biology Plasma protein binding Biology DNA-binding protein Humans Amino Acid Sequence Cyclic AMP Response Element-Binding Protein Transcription factor Chromatography High Pressure Liquid Genetics Coiled coil Leucine Zippers Multidisciplinary Circular Dichroism Temperature G-Box Binding Factors Circadian Rhythm Protein Structure Tertiary DNA-Binding Proteins Basic-Leucine Zipper Transcription Factors Thermodynamics Protein folding Peptides Dimerization Protein Binding Signal Transduction Transcription Factors |
| Zdroj: | Science (New York, N.Y.). 300(5628) |
| ISSN: | 1095-9203 |
| Popis: | In eukaryotes, the combinatorial association of sequence-specific DNA binding proteins is essential for transcription. We have used protein arrays to test 49 2 pairings of a nearly complete set of coiled-coil strands from human basic-region leucine zipper (bZIP) transcription factors. We find considerable partnering selectivity despite the bZIPs' homologous sequences. The interaction data are of high quality, as assessed by their reproducibility, reciprocity, and agreement with previous observations. Biophysical studies in solution support the relative binding strengths observed with the arrays. New associations provide insights into the circadian clock and the unfolded protein response. |
| Databáze: | OpenAIRE |
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