2cb8
From Proteopedia
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(New page: 200px<br /> <applet load="2cb8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cb8, resolution 1.40Å" /> '''HIGH RESOLUTION CRY...)
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Revision as of 19:20, 29 October 2007
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HIGH RESOLUTION CRYSTAL STRUCTURE OF LIGANDED HUMAN L-ACBP
Overview
The acyl-CoA binding protein (ACBP) is essential for the fatty acid, metabolism, membrane structure, membrane fusion, and ceramide synthesis., Here high resolution crystal structures of human cytosolic liver ACBP, unliganded and liganded with a physiological ligand, myristoyl-CoA are, described. The binding of the acyl-CoA molecule induces only few, structural differences near the binding pocket. The crystal form of the, liganded ACBP, which has two ACBP molecules in the asymmetric unit, shows, that in human ACBP the same acyl-CoA binding pocket is present as, previously described for the bovine and Plasmodium falciparum ACBP and the, mode of binding of the 3'-phosphate-AMP moiety is conserved. Unexpectedly, in one of the acyl-CoA binding pockets the acyl moiety is bound in a, reversed ... [(full description)]
About this Structure
2CB8 is a [Single protein] structure of sequence from [Homo sapiens] with ZN, SO4, MYA and MXE as [ligands]. Full crystallographic information is available from [OCA].
Reference
High resolution crystal structures of unliganded and liganded human liver ACBP reveal a new mode of binding for the acyl-CoA ligand., Taskinen JP, van Aalten DM, Knudsen J, Wierenga RK, Proteins. 2007 Jan 1;66(1):229-38. PMID:17044054
Page seeded by OCA on Mon Oct 29 21:24:47 2007
