4h32

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{STRUCTURE_4h32| PDB=4h32 | SCENE= }}
 +
===The crystal structure of the hemagglutinin H17 derived the bat influenza A virus===
 +
{{ABSTRACT_PUBMED_23434510}}
-
The entry 4h32 is ON HOLD until Paper Publication
+
==Function==
 +
[[http://www.uniprot.org/uniprot/H6QM93_9INFA H6QM93_9INFA]] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324]
-
Authors: Sun, X., Shi, Y., Lu, X., He, J., Gao, F., Yan, J., Qi, J., Gao, G.F.
+
==About this Structure==
 +
[[4h32]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/little_yellow-shouldered_bat/guatemala/060/2010(h17n10)) Influenza a virus (a/little yellow-shouldered bat/guatemala/060/2010(h17n10))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H32 OCA].
-
Description: The crystal structure of the hemagglutinin H17 derived the bat influenza A virus
+
==Reference==
 +
<ref group="xtra">PMID:023434510</ref><references group="xtra"/><references/>
 +
[[Category: Gao, F.]]
 +
[[Category: Gao, G F.]]
 +
[[Category: He, J.]]
 +
[[Category: Lu, X.]]
 +
[[Category: Qi, J.]]
 +
[[Category: Shi, Y.]]
 +
[[Category: Sun, X.]]
 +
[[Category: Yan, J.]]
 +
[[Category: Envelope of virus]]
 +
[[Category: Homotrimer]]
 +
[[Category: Viral protein]]
 +
[[Category: Virus entry and fusion]]

Revision as of 15:43, 10 July 2013

Template:STRUCTURE 4h32

Contents

The crystal structure of the hemagglutinin H17 derived the bat influenza A virus

Template:ABSTRACT PUBMED 23434510

Function

[H6QM93_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore (By similarity).[RuleBase:RU003324]

About this Structure

4h32 is a 12 chain structure with sequence from Influenza a virus (a/little yellow-shouldered bat/guatemala/060/2010(h17n10)). Full crystallographic information is available from OCA.

Reference

  • Sun X, Shi Y, Lu X, He J, Gao F, Yan J, Qi J, Gao GF. Bat-derived influenza hemagglutinin H17 does not bind canonical avian or human receptors and most likely uses a unique entry mechanism. Cell Rep. 2013 Mar 28;3(3):769-78. doi: 10.1016/j.celrep.2013.01.025. Epub 2013, Feb 21. PMID:23434510 doi:10.1016/j.celrep.2013.01.025

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4h32"
Personal tools