Ligand-gated ion channels  (Hucho & Weise, 2001) are important components of the synapse that bind neurotransmitter released from the
presynaptic cell and lead to the depolarisation of the postsynaptic cell by opening ion channels.  We are investigating the structure and the functional mechanism of the nicotinic acetylcholine receptor (nAChR) as a model for this entire category of receptor proteins. 
In this work we use protein chemical methods such as microsequencing and peptide mass spectrometry, as well as spectroscopy. Our goal is portraying the three-dimensional structure of the receptor protein with the highest possible resolution. 
 

• Heterologous expression of nAChR domains for structural investigations by CD-, FTIR- and NMR-spectroscopy (Part B3 of the SFB 449 (Structure and function of membrane-bound receptors)
• Characterisation of the ligand-binding properties of defined conformational states of the nAChR after covalent cross-linking, see Watty et al. (1997); Hucho et al. (1998); 
• Investigation of nAChR binding sites for non-competitive inhibitors, e.g. philanthotoxins (PhTXs, toxins from the wasp venom) and polymethylene-tetramines, see  Bixel et al. (2000);
• Crystallisation of the nAChR from Torpedo californica
• Kristallisierung des nAChR aus Torpedo californica 
• Acetylcholinesterase from snake venoms: The acetylcholine receptor interacts physiologically with the acetylcholinesterase (AChE); we are investigating this enzyme using biochemical and molecular biological methods. Contact:  Chris Weise