From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2bma.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2bma.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2bma| PDB=2bma | SCENE= }} | | {{STRUCTURE_2bma| PDB=2bma | SCENE= }} |
| | | | |
| - | '''THE CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM GLUTAMATE DEHYDROGENASE, A PUTATIVE TARGET FOR NOVEL ANTIMALARIAL DRUGS'''
| + | ===THE CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM GLUTAMATE DEHYDROGENASE, A PUTATIVE TARGET FOR NOVEL ANTIMALARIAL DRUGS=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Plasmodium falciparum is the main causative agent of tropical malaria, the most severe parasitic disease in the world. Growing resistance of Plasmodia towards available drugs is an increasing problem in countries where malaria is endemic. As Plasmodia are sensitive to oxidative stress, augmenting this in the parasite represents a promising principle for the development of novel antimalarial drugs. The NADP-dependent glutamate dehydrogenase (GDH) of P.falciparum is largely responsible for the production of NADPH in the parasite, which in turn serves as electron source for the antioxidative enzymes glutathione reductase and thioredoxin reductase. As GDH does not occur in the host erythrocyte, GDH is a particularly attractive target for drug therapy. The three-dimensional structure of P.falciparum GDH in the unligated state has been determined by X-ray crystallography to a resolution of 2.7A. Compared to the mammalian enzymes, two amino acid residues are exchanged in the putative active site of the parasite GDH. The most obvious differences between parasite and human GDH are the subunit interfaces of the hexameric proteins. In the parasite protein, several salt-bridges mediate contacts between the subunits whereas in the human enzyme these interactions are mainly of hydrophobic nature. Furthermore, P.falciparum GDH possesses a unique N-terminal extension that does not occur in any other GDH sequence so far studied. These findings might be exploited for the design of peptidomimetics capable of disrupting the oligomeric organisation of the parasite enzyme.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15878595}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15878595 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15878595}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| | [[Category: Plasmodium falciparum]] | | [[Category: Plasmodium falciparum]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:29:15 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:53:37 2008'' |
Revision as of 11:53, 28 July 2008
Template:STRUCTURE 2bma
THE CRYSTAL STRUCTURE OF PLASMODIUM FALCIPARUM GLUTAMATE DEHYDROGENASE, A PUTATIVE TARGET FOR NOVEL ANTIMALARIAL DRUGS
Template:ABSTRACT PUBMED 15878595
About this Structure
2BMA is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.
Reference
The crystal structure of Plasmodium falciparum glutamate dehydrogenase, a putative target for novel antimalarial drugs., Werner C, Stubbs MT, Krauth-Siegel RL, Klebe G, J Mol Biol. 2005 Jun 10;349(3):597-607. Epub 2005 Apr 12. PMID:15878595
Page seeded by OCA on Mon Jul 28 14:53:37 2008
