8VYL
The structure of Human Hemoglobin in Complex with Nanobody BtNbE11
Summary for 8VYL
| Entry DOI | 10.2210/pdb8vyl/pdb |
| Descriptor | Hemoglobin subunit alpha, Hemoglobin subunit beta, Nanobody BtNbE11, ... (6 entities in total) |
| Functional Keywords | hemoglobin, nanobody, oxygen transport |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 6 |
| Total formula weight | 95204.96 |
| Authors | Grinter, R.,Binks, S.,Fox, D. (deposition date: 2024-02-08, release date: 2024-07-17, Last modification date: 2024-10-09) |
| Primary citation | Fox, D.R.,Samuels, I.,Binks, S.,Grinter, R. The structure of a haemoglobin-nanobody complex reveals human beta-subunit-specific interactions. Febs Lett., 598:2240-2248, 2024 Cited by PubMed Abstract: Haemoglobin (Hb) is a vital oxygen carrier in vertebrates. Low blood Hb levels may indicate anaemia or genetic disorders, while its presence in the lower digestive system suggests colon cancer. Detecting and quantifying human Hb is essential for medical diagnostics. A nanobody-based sandwich-ELISA test was recently developed utilising llama-derived nanobodies NbE11 and NbB9. These nanobodies specifically bind to human Hb without cross-reacting with Hb from other vertebrates. Here, we determine the crystal structure of NbE11 in complex with human Hb. NbE11 binds Hb with high affinity, predominantly binding the β-Hb subunit. Structural differences between human Hb and other vertebrates at the NbE11 binding interface likely explain the assay's lack of cross-reactivity, providing insights for developing Hb binding diagnostics. PubMed: 38880764DOI: 10.1002/1873-3468.14958 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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