2rcu
From Proteopedia
Crystal structure of rat carnitine palmitoyltransferase 2 in complex with r-3-(hexadecanoylamino)-4-(trimethylazaniumyl)butanoate
Overview
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 1.8A 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.
About this Structure
2RCU is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Carnitine palmitoyltransferase 2: analysis of membrane association and complex structure with a substrate analog., Rufer AC, Lomize A, Benz J, Chomienne O, Thoma R, Hennig M, FEBS Lett. 2007 Jul 10;581(17):3247-52. Epub 2007 Jun 8. PMID:17585909 Page seeded by OCA on Sun May 4 16:39:22 2008
Categories: Carnitine O-palmitoyltransferase | Rattus norvegicus | Single protein | Benz, J. | Chomienne, O. | Hennig, M. | Rufer, A C. | Thoma, R. | Acetylation | Acyltransferase | Fatty acid metabolism | Inner membrane | Lipid metabolism | Membrane | Mitochondrial protein | Mitochondrion | Transferase | Transferase 04-mai-06 r | Transit peptide | Transport
