Region 1 |
Type: | Disordered |
Name: | Transactivation domain |
Location: | 545 - 713 |
Length: | 169 |
Region sequence: |
NLGIDFEDIRHMQNEKFFRNDFSGEVDFRDIDLTDEILTYVQDSLSKSPFIPSDYQQQQS LALNSSCMVQEHLHLEQQQQHHQKQVVVEPQQQLCQKMKHMQVNGMFENWNSNQFVPFNC PQQDPQQYNVFTDLHGISQEFPYKSEMDSMPYTQNFISCNQPVLPQHSK |
Modification type: | Engineered
Fragment
Monomeric
Native
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PDB: | |
Structural/functional type: | Function arises via a disorder to order transition |
Functional classes: | Modification site
Molecular recognition effectors
Molecular assembly
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Functional subclasses: | Transactivation (transcriptional activation)
Protein-protein binding
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Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (293 K; pH: 7; DTT 1 mM; Sodium phosphate (dibasic) 6 mM; Sodium phosphate (monobasic) 4 mM; Sodium sulfate 100 mM)
- Sensitivity to proteolysis
- Fourier transform infrared spectroscopy (FTIR), aka infrared spectroscopy)
- Fluorescence, intrinsic
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References:
- Watt K, Jess TJ, Kelly SM, Price NC, McEwan IJ. "Induced alpha-helix structure in the aryl hydrocarbon receptor transactivation domain modulates protein-protein interactions." Biochemistry. 2005; 44(2): 734-43. PubMed: 15641800
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Comments:
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