6IYN

Solution structure of camelid nanobody Nb26 against aflatoxin B1

Summary for 6IYN

• Entry DOI: 10.2210/pdb6iyn/pdb
• Descriptor: Nb26 (1 entity in total)
• Functional Keywords: camelid antibody, nanobody, aflatoxin b1, aflatoxin b1-binding protein
• Biological source: Vicugna pacos
• Total number of polymer chains: 1
• Total formula weight: 14527.09

Authors

Nie, Y.,He, T.,Zhu, J.,Li, S.L.,Hu, R.,Yang, Y.H. (deposition date: 2018-12-17, release date: 2019-01-23, Last modification date: 2024-05-15)

Primary citation

Nie, Y.,Li, S.,Zhu, J.,Hu, R.,Liu, M.,He, T.,Yang, Y.
Chemical shift assignments of a camelid nanobody against aflatoxin B1.
Biomol NMR Assign, 13:75-78, 2019

PubMed Abstract: Nanobodies (Nbs) are the variable domain of the heavy-chain antibodies produced from Camelidae, which possess comparable binding affinities and specificity to conventional antibodies. Nbs have become valuable and versatile tools for numerous biotechnology applications due to their small size (12-15 kDa), high solubility, exceptional stability, and facile genetic manipulation. The interactions between Nbs and protein antigens have been well-studied, but less work has been done to characterize their ability to bind small molecule haptens. Here we present the backbone and side-chain assignments of the H, C and N resonances of Nb26 (123 amino acids), a nanobody that recognizes the hapten aflatoxin B (AFB). These assignments are preliminary work towards the determination of the structure of free Nb26 using NMR spectroscopy, which will provide useful information about the complex structure of "Nb26-AFB" and the recognition mechanism about how Nb26 binds to AFB.

PubMed: 30328057
DOI: 10.1007/s12104-018-9855-y

Experimental method

SOLUTION NMR