7EH3
Structure of Nanobody Nb23 in solution using NMR spectroscopy
Summary for 7EH3
| Entry DOI | 10.2210/pdb7eh3/pdb |
| Descriptor | Nb23 (1 entity in total) |
| Functional Keywords | single-domain antibody, antibody fragment, immune system |
| Biological source | Lama glama |
| Total number of polymer chains | 1 |
| Total formula weight | 15214.81 |
| Authors | Percipalle, M.,Hunashal, Y.,Esposito, G.,Fogolari, F. (deposition date: 2021-03-28, release date: 2021-07-14, Last modification date: 2024-11-20) |
| Primary citation | Percipalle, M.,Hunashal, Y.,Steyaert, J.,Fogolari, F.,Esposito, G. Structure of Nanobody Nb23. Molecules, 26:-, 2021 Cited by PubMed Abstract: Nanobodies, or VHHs, are derived from heavy chain-only antibodies (hcAbs) found in camelids. They overcome some of the inherent limitations of monoclonal antibodies (mAbs) and derivatives thereof, due to their smaller molecular size and higher stability, and thus present an alternative to mAbs for therapeutic use. Two nanobodies, Nb23 and Nb24, have been shown to similarly inhibit the self-aggregation of very amyloidogenic variants of β2-microglobulin. Here, the structure of Nb23 was modeled with the Chemical-Shift (CS)-Rosetta server using chemical shift assignments from nuclear magnetic resonance (NMR) spectroscopy experiments, and used as prior knowledge in PONDEROSA restrained modeling based on experimentally assessed internuclear distances. Further validation was comparatively obtained with the results of molecular dynamics trajectories calculated from the resulting best energy-minimized Nb23 conformers. PubMed: 34207949DOI: 10.3390/molecules26123567 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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