6iyn

Solution structure of camelid nanobody Nb26 against aflatoxin B1

spinqualitylabelsall models 6iyn Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6iyn is a 1 chain structure with sequence from Vicugna pacos. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 (1)H, (13)C and (15)N resonances of Nb26 (123 amino acids), a nanobody that recognizes the hapten aflatoxin B1 (AFB1). 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-AFB1" and the recognition mechanism about how Nb26 binds to AFB1. Chemical shift assignments of a camelid nanobody against aflatoxin B1.,Nie Y, Li S, Zhu J, Hu R, Liu M, He T, Yang Y Biomol NMR Assign. 2019 Apr;13(1):75-78. doi: 10.1007/s12104-018-9855-y. Epub, 2018 Oct 16. PMID:30328057 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antibody 3D structures

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