1hbk: Difference between revisions

Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA, molecules in the cell and plays a role in fatty acid metabolism. The, biochemical properties of Plasmodium falciparum ACBP are described, together with the 2.0 A resolution crystal structures of a P. falciparum, ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures, published previously; however, the bovine and parasite ACBP structures are, less similar. The parasite ACBP is shown to have a different, ligand-binding pocket, leading to an acyl-CoA binding specificity, different from that of bovine ACBP. Several non-conservative differences, in residues that interact with the ligand were identified between the, mammalian and parasite ACBPs. These, together with measured, binding-specificity differences, suggest that there is a potential for the, design of molecules that might selectively block the acyl-CoA binding, site.

1HBK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] with NI, COA and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: COA, MYR, NI1 and NI2. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBK OCA].  

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