Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050746 | FEBS Letters | 2007 | 6 Pages |
Abstract
The mitochondrial membrane-associated carnitine palmitoyltransferase system is a validated target for the treatment of type 2 diabetes mellitus. To further facilitate structure-based drug discovery, we determined the crystal structure of rat CPT-2 (rCPT-2) in complex with the substrate analogue palmitoyl-aminocarnitine at 1.8 Å resolution. Biochemical analyses revealed a strong effect of this compound on rCPT-2 activity and stability. Using a computational approach we examined the membrane association of rCPT-2. The protein interacts with the membrane as a functional monomer and the calculations confirm the presence of a membrane association domain that consists of layers of hydrophobic and positively charged residues.
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Authors
Arne C. Rufer, Andrei Lomize, Jörg Benz, Odile Chomienne, Ralf Thoma, Michael Hennig,