| + |
BOLA2 | form complex 
binding
|
BOLA2-GLRX3 iron-sulfur cluster assembly complex |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281068 |
|
|
|
|
| pmid |
sentence |
| 22309771 |
Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. |
|
| Publications: |
1 |
| + |
GLRX3 | form complex
binding
|
BOLA2-GLRX3 iron-sulfur cluster assembly complex |
0.576 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281067 |
|
|
|
|
| pmid |
sentence |
| 22309771 |
Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. |
|
| Publications: |
1 |
| + |
BOLA2-GLRX3 iron-sulfur cluster assembly complex | up-regulates quantity 
chemical modification
|
iron-sulfur cluster |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281069 |
|
|
|
|
| pmid |
sentence |
| 22309771 |
Herein, we provide biophysical and biochemical evidence that the two tandem Grx-like domains in human Glrx3 form similar [2Fe-2S]-bridged complexes with human BolA2. Furthermore, we demonstrate that apo BolA2 binds to each Grx domain in the [2Fe-2S] Glrx3 homodimer forming a [2Fe-2S] BolA2-Glrx3 heterotrimer. Taken together, these results suggest that the unusual [2Fe-2S]-bridging Grx-BolA interaction is conserved in higher eukaryotes and may play a role in signaling cellular iron status in humans. |
|
| Publications: |
1 |
4.0
BOLA2-GLRX3 iron-sulfur cluster assembly complex