6ITQ
Crystal structure of cortisol complexed with its nanobody at pH 10.5
Summary for 6ITQ
| Entry DOI | 10.2210/pdb6itq/pdb |
| Descriptor | anti-cortisol camelid antibody, (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | cortisol, complex, nanobody, camelid antibody, immune system |
| Biological source | Camelus bactrianus |
| Total number of polymer chains | 4 |
| Total formula weight | 56762.35 |
| Authors | Ding, Y.,Ding, L.L.,Wang, Z.Y.,Zhong, P.Y. (deposition date: 2018-11-24, release date: 2019-07-24, Last modification date: 2023-11-22) |
| Primary citation | Ding, L.,Wang, Z.,Zhong, P.,Jiang, H.,Zhao, Z.,Zhang, Y.,Ren, Z.,Ding, Y. Structural insights into the mechanism of single domain VHH antibody binding to cortisol. Febs Lett., 593:1248-1256, 2019 Cited by PubMed Abstract: To date, few structural models of VHH antibody binding to low molecular weight haptens have been reported. Here, we report the crystal structure of cortisol binding to its VHH antibody NbCor at pH 3.5 and 10.5. Cortisol binds to NbCor mainly by burying itself under the tunnel formed by the complementarity determining region 1 (CDR1) of NbCor. The affinity of NbCor binding to cortisol and similar compounds was also verified by a microscale thermophoresis assay. Combining our findings with several previously reported structures of hapten-VHH antibody complexes, we propose that VHH antibodies exhibit a special mechanism of binding small haptens by encapsulating them in a tunnel formed by CDR1. Our findings provide useful structural information for the further development and optimization of hapten-specific VHH antibodies. PubMed: 31049949DOI: 10.1002/1873-3468.13398 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.526 Å) |
Structure validation
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