| Autor: |
Vuchelen A; Department of Chemistry, University of Cambridge, Cambridge, UK., O'Day E, De Genst E, Pardon E, Wyns L, Dumoulin M, Dobson CM, Christodoulou J, Hsu ST |
| Jazyk: |
angličtina |
| Zdroj: |
Biomolecular NMR assignments [Biomol NMR Assign] 2009 Dec; Vol. 3 (2), pp. 231-3. |
| DOI: |
10.1007/s12104-009-9182-4 |
| Abstrakt: |
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 approximately 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 alpha-synuclein (aS), whose aberrant self-association is implicated in Parkinson's disease. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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