| + |
Hemoglobin | form complex 
binding
|
hb:hp |
0.723 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255284 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11854029 |
CD163 was identified as the endocytic receptor binding hemoglobin (Hb) in complex with the plasma protein haptoglobin (Hp). This specific receptor-ligand interaction leading to removal from plasma of the Hp-Hb complex-but not free Hp or Hb-now explains the depletion of circulating Hp in individuals with increased intravascular hemolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HBB | form complex
binding
|
Hemoglobin |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255275 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18179859 |
AHSP does not bind to β-hemoglobin (βHb) or the hemoglobin tetramer, instead, it specifically binds to free αHb, avoiding its precipitation and its pro-oxidant activity. In the presence of βHb, the αHb-AHSP complex is dismembered and βHb displaces AHSP to generate the quaternary structure of hemoglobin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HBA1 | form complex
binding
|
Hemoglobin |
0.698 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255274 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18179859 |
AHSP does not bind to β-hemoglobin (βHb) or the hemoglobin tetramer, instead, it specifically binds to free αHb, avoiding its precipitation and its pro-oxidant activity. In the presence of βHb, the αHb-AHSP complex is dismembered and βHb displaces AHSP to generate the quaternary structure of hemoglobin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
Hemoglobin
CPX-2158