This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2ghu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ghu.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2ghu.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ghu| PDB=2ghu | SCENE= }}
{{STRUCTURE_2ghu| PDB=2ghu | SCENE= }}
-
'''Crystal structure of falcipain-2 from Plasmodium falciparum'''
+
===Crystal structure of falcipain-2 from Plasmodium falciparum===
-
==Overview==
+
<!--
-
Malaria is caused by protozoan erythrocytic parasites of the Plasmodium genus, with Plasmodium falciparum being the most dangerous and widespread disease-causing species. Falcipain-2 (FP-2) of P. falciparum is a papain-family (C1A) cysteine protease that plays an important role in the parasite life cycle by degrading erythrocyte proteins, most notably hemoglobin. Inhibition of FP-2 and its paralogues prevents parasite maturation, suggesting these proteins may be valuable targets for the design of novel antimalarial drugs, but lack of structural knowledge has impeded progress toward the rational discovery of potent, selective, and efficacious inhibitors. As a first step toward this goal, we present here the crystal structure of mature FP-2 at 3.1 A resolution, revealing novel structural features of the FP-2 subfamily proteases including a dynamic beta-hairpin hemoglobin binding motif, a flexible N-terminal alpha-helical extension, and a unique active-site cleft. We also demonstrate by biochemical methods that mature FP-2 can proteolytically process its own precursor in trans at neutral to weakly alkaline pH, that the binding of hemoglobin to FP-2 is strictly pH-dependent, and that FP-2 preferentially binds methemoglobin over hemoglobin. Because the specificity and proteolytic activity of FP-2 toward its multiple targets appears to be pH-dependent, we suggest that environmental pH may play an important role in orchestrating FP-2 function over the different life stages of the parasite. Moreover, it appears that selectivity of FP-2 for methemoglobin may represent an evolutionary adaptation to oxidative stress conditions within the host cell.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16777845}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16777845 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16777845}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Random coil]]
[[Category: Random coil]]
[[Category: Twisted antiparallel beta-sheet]]
[[Category: Twisted antiparallel beta-sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:07:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:53:18 2008''

Revision as of 02:53, 28 July 2008

Image:2ghu.png

Template:STRUCTURE 2ghu

Crystal structure of falcipain-2 from Plasmodium falciparum

Template:ABSTRACT PUBMED 16777845

About this Structure

2GHU is a Single protein structure of sequence from Plasmodium falciparum. Full crystallographic information is available from OCA.

Reference

Structural and functional characterization of Falcipain-2, a hemoglobinase from the malarial parasite Plasmodium falciparum., Hogg T, Nagarajan K, Herzberg S, Chen L, Shen X, Jiang H, Wecke M, Blohmke C, Hilgenfeld R, Schmidt CL, J Biol Chem. 2006 Sep 1;281(35):25425-37. Epub 2006 Jun 15. PMID:16777845

Page seeded by OCA on Mon Jul 28 05:53:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ghu"
Personal tools