1hbk

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{{STRUCTURE_1hbk| PDB=1hbk | SCENE= }}
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'''ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM'''
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===ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11491287 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11491287}}
==About this Structure==
==About this Structure==
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[[Category: Aalten, D M.F Van.]]
[[Category: Aalten, D M.F Van.]]
[[Category: Fatty acid metabolism]]
[[Category: Fatty acid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 07:56:37 2008''

Revision as of 04:56, 1 July 2008

Image:1hbk.png

Template:STRUCTURE 1hbk

ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM

Template:ABSTRACT PUBMED 11491287

About this Structure

Full crystallographic information is available from OCA.

Reference

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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