1oc4: Difference between revisions

Revision as of 16:09, 29 July 2008

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File:1oc4.png

Template:STRUCTURE 1oc4

LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEILACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI

Template:ABSTRACT PUBMED 12967707

About this StructureAbout this Structure

1OC4 is a Single protein structure of sequence from Plasmodium berghei. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of Plasmodium berghei lactate dehydrogenase indicates the unique structural differences of these enzymes are shared across the Plasmodium genus., Winter VJ, Cameron A, Tranter R, Sessions RB, Brady RL, Mol Biochem Parasitol. 2003 Sep;131(1):1-10. PMID:12967707

Page seeded by OCA on Tue Jul 29 16:09:41 2008

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OCA

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-[[Image:1oc4.gif|left|200px]]
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 {{STRUCTURE_1oc4|  PDB=1oc4  |  SCENE=  }}
-'''LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI'''
+===LACTATE DEHYDROGENASE FROM PLASMODIUM BERGHEI===
-==Overview==
+<!--
-As Plasmodium rely extensively on homolactic fermentation for energy production, Plasmodium falciparum lactate dehydrogenase (PfLDH)--the key enzyme in this process--has previously been suggested as a novel target for antimalarials. This enzyme has distinctive kinetic and structural properties that distinguish it from its human homologues. In this study, we now describe the expression, kinetic characterisation and crystal structure determination of the LDH from Plasmodium berghei. This enzyme is seen to have a similar kinetic profile to its P. falciparum counterpart, exhibiting the characteristic lack of substrate inhibition that distinguishes plasmodial from human LDHs. The crystal structure of P. berghei lactate dehydrogenase (PbLDH) shows a very similar active site arrangement to the P. falciparum enzyme. In particular, an insertion of five amino acid residues in the active site loop creates an enlarged volume in the substrate binding site, and characteristic changes in the residues lining the NADH cofactor binding pocket result in displacement of the cofactor relative to its observed position in mammalian and all other LDH structures. These results imply the special features previously described for PfLDH may be shared across the Plasmodium genus, supporting the universal application of therapeutics targeting this enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_12967707}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12967707 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12967707}}
 ==About this Structure==
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 [[Category: Lactate dehydrogenase]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:39:09 2008''
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