1hbk: Difference between revisions
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==Overview== | ==Overview== | ||
Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Aalten, D | [[Category: Aalten, D M.F Van.]] | ||
[[Category: COA]] | [[Category: COA]] | ||
[[Category: MYR]] | [[Category: MYR]] | ||
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[[Category: fatty acid metabolism]] | [[Category: fatty acid metabolism]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:59:28 2008'' | ||
Revision as of 13:59, 21 February 2008
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ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM
OverviewOverview
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.
About this StructureAbout this Structure
1HBK is a Protein complex structure of sequences from Plasmodium falciparum with , and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein., van Aalten DM, Milne KG, Zou JY, Kleywegt GJ, Bergfors T, Ferguson MA, Knudsen J, Jones TA, J Mol Biol. 2001 May 25;309(1):181-92. PMID:11491287
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