Structural and biophysical characterisation of agrin laminin G3 domain constructs

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Agrin mediates accumulation of acetylcholine receptors (AChRs) at the developing neuromuscular junction, but has also been implicated as a regulator of central nervous system (CNS) synapses. A C-terminal region of agrin (Ag-C20) binds to the α3 subunit of the sodium-potassium ATPase (NKA) in CNS neurons suggesting that α3NKA is a neuronal agrin receptor, whereas a shorter agrin fragment (Ag-C15) was shown to act as a competitive antagonist. Here, we show that the agrin C22 construct, which represents the naturally occurring neurotrypsin cleavage product, constitutes a well-folded, stable domain, while the deletion of 48 residues that correspond to strands β1-β4 of the agrin laminin G3 domain imposed by the agrin C15 construct leads to a misfolded protein.
OriginalsprogEngelsk
TidsskriftProtein Engineering Design and Selection (Print)
Vol/bind24
Nummer1-2
Sider (fra-til)219-224
Antal sider6
ISSN1741-0126
DOI
StatusUdgivet - 2011

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