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.


1ztx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ztx.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ztx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ztx| PDB=1ztx | SCENE= }}
{{STRUCTURE_1ztx| PDB=1ztx | SCENE= }}
-
'''West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab'''
+
===West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab===
-
==Overview==
+
<!--
-
West Nile virus is a mosquito-borne flavivirus closely related to the human epidemic-causing dengue, yellow fever and Japanese encephalitis viruses. In establishing infection these icosahedral viruses undergo endosomal membrane fusion catalysed by envelope glycoprotein rearrangement of the putative receptor-binding domain III (DIII) and exposure of the hydrophobic fusion loop. Humoral immunity has an essential protective function early in the course of West Nile virus infection. Here, we investigate the mechanism of neutralization by the E16 monoclonal antibody that specifically binds DIII. Structurally, the E16 antibody Fab fragment engages 16 residues positioned on four loops of DIII, a consensus neutralizing epitope sequence conserved in West Nile virus and distinct in other flaviviruses. The E16 epitope protrudes from the surface of mature virions in three distinct environments, and docking studies predict Fab binding will leave five-fold clustered epitopes exposed. We also show that E16 inhibits infection primarily at a step after viral attachment, potentially by blocking envelope glycoprotein conformational changes. Collectively, our results suggest that a vaccine strategy targeting the dominant DIII epitope may elicit safe and effective immune responses against flaviviral diseases.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16193056}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16193056 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16193056}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Neutralizing]]
[[Category: Neutralizing]]
[[Category: Virus]]
[[Category: Virus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:04:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:33:31 2008''

Revision as of 10:33, 28 July 2008

Image:1ztx.png

Template:STRUCTURE 1ztx

West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab

Template:ABSTRACT PUBMED 16193056

About this Structure

1ZTX is a Single protein structure of sequence from Mus musculus and West nile virus. Full crystallographic information is available from OCA.

Reference

Structural basis of West Nile virus neutralization by a therapeutic antibody., Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH, Nature. 2005 Sep 29;437(7059):764-9. PMID:16193056

Page seeded by OCA on Mon Jul 28 13:33:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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