Structural highlights
Publication Abstract from PubMed
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.
Structural insights into the mechanism of single domain VHH antibody binding to cortisol.,Ding L, Wang Z, Zhong P, Jiang H, Zhao Z, Zhang Y, Ren Z, Ding Y FEBS Lett. 2019 Jun;593(11):1248-1256. doi: 10.1002/1873-3468.13398. Epub 2019, May 20. PMID:31049949[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ 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. 2019 Jun;593(11):1248-1256. doi: 10.1002/1873-3468.13398. Epub 2019, May 20. PMID:31049949 doi:http://dx.doi.org/10.1002/1873-3468.13398
