We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1pa3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1pa3.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1pa3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1pa3| PDB=1pa3 | SCENE= }}
{{STRUCTURE_1pa3| PDB=1pa3 | SCENE= }}
-
'''Crystal Structure of Glutathione-S-transferase from Plasmodium falciparum'''
+
===Crystal Structure of Glutathione-S-transferase from Plasmodium falciparum===
-
==Overview==
+
<!--
-
The parasite Plasmodium falciparum causes malaria tropica, the most prevailing parasitic disease worldwide, with 300-500 million infections and 1.5-2.7 million deaths/year. The emergence of strains resistant to drugs used for prophylaxis and treatment and no vaccine available makes the structural analysis of potential drug targets essential. For that reason, we analyzed the three-dimensional structure of the glutathione S-transferase from P. falciparum (Pf-GST1) in the apoform and in complex with its inhibitor S-hexyl-glutathione. The structures have been analyzed to 2.6 and 2.2 A, respectively. Pf-GST1 shares several structural features with the Mu-type GSTs and is therefore closely related to this class, even though alignments with its members display low sequence identities in the range of 20-33%. Upon S-hexyl-glutathione binding, the overall structure and the glutathione-binding site (G-site) remain almost unchanged with the exception of the flexible C terminus. The detailed comparison of the parasitic enzyme with the human host Mu-class enzyme reveals that, although the overall structure is homologue, the shape of the hydrophobic binding pocket (H-site) differs substantially. In the human enzyme, it is shielded from one side by the large Mu-loop, whereas in Pf-GST1 the Mu-loop is truncated and the space to recognize and bind voluminous substrates is extended. This structural feature can be exploited to support the design of specific and parasite-selective inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12972411}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12972411 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12972411}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Perbandt, M.]]
[[Category: Perbandt, M.]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:52:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:48:12 2008''

Revision as of 02:48, 28 July 2008

Image:1pa3.png

Template:STRUCTURE 1pa3

Crystal Structure of Glutathione-S-transferase from Plasmodium falciparum

Template:ABSTRACT PUBMED 12972411

About this Structure

1PA3 is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.

Reference

Native and inhibited structure of a Mu class-related glutathione S-transferase from Plasmodium falciparum., Perbandt M, Burmeister C, Walter RD, Betzel C, Liebau E, J Biol Chem. 2004 Jan 9;279(2):1336-42. Epub 2003 Sep 12. PMID:12972411

Page seeded by OCA on Mon Jul 28 05:48:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1pa3"
Personal tools