1tw9: Difference between revisions
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[[Image: | ==Glutathione Transferase-2, apo form, from the nematode Heligmosomoides polygyrus== | ||
<StructureSection load='1tw9' size='340' side='right' caption='[[1tw9]], [[Resolution|resolution]] 1.71Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1tw9]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Heligmosomoides_polygyrus Heligmosomoides polygyrus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TW9 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tw9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1tw9 RCSB], [http://www.ebi.ac.uk/pdbsum/1tw9 PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tw/1tw9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of GST Nu2-2 (HpolGSTN2-2) from the model hookworm nematode Heligmosomoides polygyrus has been solved by the molecular replacement method and refined to a resolution of 1.71 A, providing the first structural data from a class of nematode-specific GSTs. By structural alignment with two Sigma class GSTs, glutathione could be rationally docked into the G-site of the enzyme. By comparing with all mammalian GST classes, a novel, long, and deep cleft was identified at the H-site, providing a potential site for ligand binding. This new GST class may support the establishment of infection parasitic nematodes by passively neutralizing chemical toxins derived from host environment. The structure serves as a starting point for structure-based drug/inhibitor design that would aim to selectively disrupt nematode chemical defenses. | |||
Crystal structure of a new class of glutathione transferase from the model human hookworm nematode Heligmosomoides polygyrus.,Schuller DJ, Liu Q, Kriksunov IA, Campbell AM, Barrett J, Brophy PM, Hao Q Proteins. 2005 Dec 1;61(4):1024-31. PMID:16189827<ref>PMID:16189827</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Glutathione S-transferase|Glutathione S-transferase]] | *[[Glutathione S-transferase|Glutathione S-transferase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Heligmosomoides polygyrus]] | [[Category: Heligmosomoides polygyrus]] | ||
[[Category: Barrett, J.]] | [[Category: Barrett, J.]] | ||
Revision as of 19:18, 29 September 2014
Glutathione Transferase-2, apo form, from the nematode Heligmosomoides polygyrus
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