1tu7

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[[Image:1tu7.gif|left|200px]]
[[Image:1tu7.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1tu7 |SIZE=350|CAPTION= <scene name='initialview01'>1tu7</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1tu7", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GTT:GLUTATHIONE'>GTT</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= GST2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6282 Onchocerca volvulus])
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-->
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|DOMAIN=
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{{STRUCTURE_1tu7| PDB=1tu7 | SCENE= }}
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|RELATEDENTRY=[[1tu8|1TU8]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu7 OCA], [http://www.ebi.ac.uk/pdbsum/1tu7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tu7 RCSB]</span>
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}}
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'''Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase'''
'''Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Perbandt, M.]]
[[Category: Perbandt, M.]]
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[[Category: transferase]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:22:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:07 2008''
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Revision as of 07:22, 3 May 2008

Template:STRUCTURE 1tu7

Structure of Onchocerca Volvulus Pi-class Glutathione S-transferase


Overview

Onchocerciasis is a debilitating parasitic disease caused by the filarial worm Onchocerca volvulus. Similar to other helminth parasites, O. volvulus is capable of evading the host's immune responses by a variety of defense mechanisms, including the detoxification activities of the glutathione S-transferases (GSTs). Additionally, in response to drug treatment, helminth GSTs are highly up-regulated, making them tempting targets both for chemotherapy and for vaccine development. We analyzed the three-dimensional x-ray structure of the major cytosolic GST from O. volvulus (Ov-GST2) in complex with its natural substrate glutathione and its competitive inhibitor S-hexylglutathione at 1.5 and 1.8 angstrom resolution, respectively. From the perspective of the biochemical classification, the Ov-GST2 seems to be related to pi-class GSTs. However, in comparison to other pi-class GSTs, in particular to the host's counterpart, the Ov-GST2 reveals significant and unusual differences in the sequence and overall structure. Major differences can be found in helix alpha-2, an important region for substrate recognition. Moreover, the binding site for the electrophilic co-substrate is spatially increased and more solvent-accessible. These structural alterations are responsible for different substrate specificities and will form the basis of parasite-specific structure-based drug design investigations.

About this Structure

1TU7 is a Single protein structure of sequence from Onchocerca volvulus. Full crystallographic information is available from OCA.

Reference

Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus., Perbandt M, Hoppner J, Betzel C, Walter RD, Liebau E, J Biol Chem. 2005 Apr 1;280(13):12630-6. Epub 2005 Jan 7. PMID:15640152 Page seeded by OCA on Sat May 3 10:22:16 2008

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