1H, 13C and 15N assignments of a camelid nanobody directed against human α-synuclein
Vuchelen, A. and O’Day, E. and de Genst, E. and Pardon, E. and Lode Wyns, L. and Dobson, C.M. and Christodoulou, John and Hsu, S.T.D. (2009) 1H, 13C and 15N assignments of a camelid nanobody directed against human α-synuclein. Biomolecular Nmr Assignments 3 (2), pp. 231-233. ISSN 1874-2718.
Nanobodies are single chain antibodies that are uniquely produced in Camelidae, e.g. camels and llamas. They have the desirable features of small sizes (Mw < 14 kDa) and high affinities against antigens (Kd ~ nM), making them ideal as structural probes for biomedically relevant motifs both in vitro and in vivo. We have previously shown that nanobody binding to amyloidogenic human lysozyme variants can effectively inhibit their aggregation, the process that is at the origin of systemic amyloid disease. Here we report the NMR assignments of a new nanobody, termed NbSyn2, which recognises the C-terminus of the intrinsically disordered protein, human α-synuclein (aS), whose aberrant self-association is implicated in Parkinson’s disease.
|School:||Birkbeck Schools and Departments > School of Science > Biological Sciences|
|Research Centre:||Structural Molecular Biology, Institute of (ISMB)|
|Date Deposited:||04 Aug 2010 14:09|
|Last Modified:||06 Dec 2016 10:48|
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