Difference between revisions of "Part:BBa K3128021"
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<partinfo>BBa_K3128021 short</partinfo> | <partinfo>BBa_K3128021 short</partinfo> | ||
| − | Leucine zipper are known to interact by forming homodimers. | + | Leucine zipper are known to interact by forming homodimers. They contain two different motifs : a basic region recognizing a specific DNA sequence and a periodic repetition with a leucine residue placed at every seventh position. Their secondary structure forms an alpha helical conformation allowing to dimerize themselves more easily.In the Neurodrop project, this caracteristic was used to bring closer two transmembrane OMPx proteins. |
Latest revision as of 19:05, 8 October 2019
Leucine Zipper
Leucine zipper are known to interact by forming homodimers. They contain two different motifs : a basic region recognizing a specific DNA sequence and a periodic repetition with a leucine residue placed at every seventh position. Their secondary structure forms an alpha helical conformation allowing to dimerize themselves more easily.In the Neurodrop project, this caracteristic was used to bring closer two transmembrane OMPx proteins.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 41