Relation Results

Summary

Name Hemoglobin
Primary ID SIGNOR-C209
Links CPX-2158
Type complex
Formed by HBB, HBA1
Relations 3

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Type: Score: Layout: SPV 
0.6990.750.699HBA1Hemoglobinhb:hpHBB

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Relations
Regulator
Mechanism
target
score ℹ
+ HBA1form complex img/form-complex.png binding Hemoglobin 0.699
Identifier Residue Sequence Organism Cell Line
SIGNOR-255274 Homo sapiens
pmid sentence
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
+ Hemoglobinform complex img/form-complex.png binding hb:hp 0.75
Identifier Residue Sequence Organism Cell Line
SIGNOR-255284 Homo sapiens
pmid sentence
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
+ HBBform complex img/form-complex.png binding Hemoglobin 0.699
Identifier Residue Sequence Organism Cell Line
SIGNOR-255275 Homo sapiens
pmid sentence
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
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