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.


2pn5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pn5.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2pn5.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pn5| PDB=2pn5 | SCENE= }}
{{STRUCTURE_2pn5| PDB=2pn5 | SCENE= }}
-
'''Crystal Structure of TEP1r'''
+
===Crystal Structure of TEP1r===
-
==Overview==
+
<!--
-
Thioester-containing proteins (TEPs) are a major component of the innate immune response of insects to invasion by bacteria and protozoa. TEPs form a distinct clade of a superfamily that includes the pan-protease inhibitors alpha(2)-macroglobulins and vertebrate complement factors. The essential feature of these proteins is a sequestered thioester bond that, after cleavage in a protease-sensitive region of the protein, is activated and covalently binds to its target. Recently, TEP1 from the malarial vector Anopheles gambiae was shown to mediate recognition and killing of ookinetes from the malarial parasite Plasmodium berghei, a model for the human malarial parasite Plasmodium falciparum. Here, we present the crystal structure of the TEP1 isoform TEP1r. Although the overall protein fold of TEP1r resembles that of complement factor C3, the TEP1r domains are repositioned to stabilize the inactive conformation of the molecule (containing an intact thioester) in the absence of the anaphylotoxin domain, a central component of complement factors. The structure of TEP1r provides a molecular basis for the differences between TEP1 alleles TEP1r and TEP1s, which correlate with resistance of A. gambiae to infection by P. berghei.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17606907}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17606907 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17606907}}
==About this Structure==
==About this Structure==
Line 22: Line 26:
[[Category: Baxter, R H.G.]]
[[Category: Baxter, R H.G.]]
[[Category: Full-length mature peptide]]
[[Category: Full-length mature peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:27:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:45:50 2008''

Revision as of 08:45, 28 July 2008

Image:2pn5.png

Template:STRUCTURE 2pn5

Crystal Structure of TEP1r

Template:ABSTRACT PUBMED 17606907

About this Structure

Full crystallographic information is available from OCA.

Reference

Structural basis for conserved complement factor-like function in the antimalarial protein TEP1., Baxter RH, Chang CI, Chelliah Y, Blandin S, Levashina EA, Deisenhofer J, Proc Natl Acad Sci U S A. 2007 Jul 10;104(28):11615-20. Epub 2007 Jul 2. PMID:17606907

Page seeded by OCA on Mon Jul 28 11:45:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pn5"
Personal tools