1hbk: Difference between revisions

Revision as of 07:56, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1hbk.png

Template:STRUCTURE 1hbk

ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUMACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM

Template:ABSTRACT PUBMED 11491287

About this StructureAbout this Structure

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

Page seeded by OCA on Tue Jul 1 07:56:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1hbk.gif|left|200px]]
+{{Seed}}
+[[Image:1hbk.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1hbk|  PDB=1hbk  |  SCENE=  }}
-'''ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM'''
+===ACYL-COA BINDING PROTEIN FROM PLASMODIUM FALCIPARUM===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11491287}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11491287 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11491287}}
 ==About this Structure==
@@ Line 22: / Line 26: @@
 [[Category: Aalten, D M.F Van.]]
 [[Category: Fatty acid metabolism]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:40:10 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 07:56:37 2008''