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.


1lee

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1lee.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1lee.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1lee| PDB=1lee | SCENE= }}
{{STRUCTURE_1lee| PDB=1lee | SCENE= }}
-
'''CRYSTAL STRUCTURE OF PLASMEPSIN FROM P. FALCIPARUM IN COMPLEX WITH INHIBITOR RS367'''
+
===CRYSTAL STRUCTURE OF PLASMEPSIN FROM P. FALCIPARUM IN COMPLEX WITH INHIBITOR RS367===
-
==Overview==
+
<!--
-
Plasmepsin II is one of the four catalytically active plasmepsins found in the food vacuole of Plasmodium falciparum. These enzymes initiate hemoglobin degradation by cleavage at the alpha-chain between Phe33 and Leu34. The crystal structures of Ser205 mutant plasmepsin II from P. falciparum in complex with two inhibitors have been refined at a resolution of 1.8 A in the space group I222 and to R factors of 19.9 and 19.5%. Each crystal contains one monomer in the asymmetric unit. Both inhibitors have a Phe-Leu core and incorporate tetrahedral transition-state mimetic hydroxypropylamine. The inhibitor rs367 possesses a 2,6-dimethylphenyloxyacetyl group at the P2 position and 3-aminobenzamide at the P2' position, while rs370 has the same P2 group but 4-aminobenzamide in the P2' position. These complexes reveal key conserved hydrogen bonds between the inhibitor and the binding-cavity residues, notably with the flap residues Val78 and Ser79, the catalytic dyad Asp34 and Asp214 and the residues Ser218 and Gly36 that are in proximity to the catalytic dyad. The structures also show unexpected conformational variability of the binding cavity of plasmepsin II and may reflect the mode of binding of the hemoglobin alpha-chain for cleavage.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12454457}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12454457 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12454457}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Plasmepsin]]
[[Category: Plasmepsin]]
[[Category: Plasmodium falciparum]]
[[Category: Plasmodium falciparum]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:50:36 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 13:51:48 2008''

Revision as of 11:09, 2 July 2008

Image:1lee.png

Template:STRUCTURE 1lee

CRYSTAL STRUCTURE OF PLASMEPSIN FROM P. FALCIPARUM IN COMPLEX WITH INHIBITOR RS367

Template:ABSTRACT PUBMED 12454457

About this Structure

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

Reference

Structures of Ser205 mutant plasmepsin II from Plasmodium falciparum at 1.8 A in complex with the inhibitors rs367 and rs370., Asojo OA, Afonina E, Gulnik SV, Yu B, Erickson JW, Randad R, Medjahed D, Silva AM, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2001-8. Epub 2002, Nov 23. PMID:12454457

Page seeded by OCA on Wed Jul 2 13:51:48 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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